WATER – ITS PROPERTIES AND IMPORTANCE

1.1 : understand the importance of water as a solvent in transport, including its dipole nature
It is a covalent compound of hydrogen and oxygen.
Hydrogen atom is having a slight positive charge (δ+) and oxygen atom is having a slight negative
(δ-) charge.
It is dipolar in nature.
Water molecules form hydrogen bond between them.
Water has high melting and boiling point because of this hydrogen bonding between them.

POLARITY OF WATER MOLECULE

Because oxygen is more electronegative, the region around oxygen has a partial negative charge.
The region near the two hydrogen atoms has a partial positive charge.
A water molecule is a polar molecule with opposite ends of the molecule with opposite charges (hydrogen
atom with partial positive and oxygen with partial negative charge).

Properties of water

1) Unusual and excellent solvent

2) High surface tension

3) High latent heat of vaporization

4) High specific heat capacity

5) Density

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Universal solvent
Almost all the substances will dissolve in water due to its dipolar nature. All the polar or ionic substances
dissolve in water. These substances can form hydrogen bond with water.
It can form colloids (solute particles are larger than solvent) with non-polar substances.
It can form emulsion (liquid liquid) or suspension (liquid solid)
Dissolving sodium chloride in water

NaCl dissolve in water. The positive and negative ions of sodium chloride separate and become
surrounded by water molecules which keep them in solution.

Slightly negative Oxygen atom of the water molecules are attracted by the positively charged
sodium ions and slightly positive hydrogen atoms are attracted by the negatively charged chloride
ions.

How the dipolar nature of water is essential for living organisms.

Water can form hydrogen bonds

Water is a solvent and polar molecule can dissolve in water and can be transported.
Cohesion and adhesion lead to high surface tension
Hydrogen bonds holding water together as a liquid, so that it can move in mass flow systems
Has high specific heat capacity and high latent heat of vaporisation.
This helps to maintain body temperature without much fluctuation
The polarity of water allows it to dissolve other polar molecules.

High surface tension

The property of the liquid where it behaves like a stretched membrane.

High surface tension of water is due to the presence of hydrogen bonds
It is of great importance in plant transport systems and also affects life at the surface of ponds, lakes and
other water masses.

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Water behaves as if covered by an invisible film
Some animals can stand, walk, or run on water without breaking the surface.
This provides an excellent capillary action.

High latent heat of vaporization

It is the amount of heat energy needed to convert 1kg of water to its vapour state at a constant
temperature.
This property of water makes it a good coolant, as it absorbs heat from the body to evaporate.
Helps stabilize temperatures in organisms and bodies of water
Prevent organisms from Overheating.

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High latent heat of fusion

It is the amount of heat energy needed to convert 1kg of ice into water or water into ice at constant
temperature.
It ensures that water bodies do not freeze easily in cold climate.
Prevent cytoplasm from freezing at low temperatures.
Density and freezing properties
Most dense at 4oC
Contracts until 4oC
On further cooling it expands from 4oC to 0oC
Ice is less dense than water and tends to float on water

Prevent water from freezing from the bottom up.

Ice forms on the surface first—the freezing of the water
releases heat to the water below creating insulation.
It reduces heat loss from the water body
It allows aquatic organisms to live underneath

High specific heat capacity

This is the amount of heat energy needed to increase the temperature of 1 kg of water by 1°C. (4200J/kg)
For a small change in temperature it needs to add or remove a lot of heat.
This prevents sudden fluctuations in temperature of aquatic environments.
This is extremely useful for organisms,
Helping them to avoid rapid changes in their internal temperature
Enabling them to maintain a steady temperature even when the temperature in their surroundings varies
considerably.

4
Why water is an effective molecule for transporting other molecules around living organisms.

Water is a solvent
Water is slightly charged / dipolar
Polar molecules can dissolve in water by the formation of hydrogen bond with water
Cohesion / adhesion leads to high surface tension which help in plant transport system
Water as a liquid assist in mass flow

WRITE THE ANSWERS

Water molecules are described as ................................................. because they have a slight positive
charge at one end of the molecule and a slight negative charge at the other end. This makes water a
good ................................................. for salts and substances such as sugars. Bonds that form
between water molecules are called ................................................. bonds. Water is a good coolant
because it has a high ................................................., which means that it takes a lot of heat to
change it from a liquid to a gas. Water also has a high .................................................. , which
means that a lot of energy is needed to cause a small rise in its temperature.

So floats on surface to provide a habitat to live on.

Insulation of water so life can survive when ice forms

High latent heat of vapourisation

Allows movement through xylem. (transpiration

stream).

Surface tension allows insects to walk/ live on water

surface

High specific heat capacity

Used for transport/ movement of molecules/

metabolic reactions occur in solution

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MACROMOLECULES
SPECIFICATION
(i) know the difference between monosaccharides, disaccharides
and polysaccharides, including glycogen and starch (amylose
and amylopectin)
(ii) be able to relate the structures of monosaccharides,
disaccharides and polysaccharides to their roles in providing and storing energy
β-glucose and cellulose are not required in this topic.
know how monosaccharides (glucose, fructose and galactose) join together to form
disaccharides (maltose, sucrose and lactose) and polysaccharides (glycogen, amylose and
amylopectin) through condensation reactions forming glycosidic bonds, and how these can
be split through hydrolysis reactions.
Carbohydrates
These are compounds made up of carbon, hydrogen and oxygen.
It is important in organisms as an energy source.
Its general formula is Cn(H2O)n /(CH2O)n.
It can be classified into two main groups- sugars and polysaccharides.
Sugars can be divided further into monosaccharide and disaccharides.
Classification of carbohydrates

Monosaccharide
These are single sugar units with the general formula (CH2O) n/ CnH2nOn
They are the simple sugars. They have between three and seven carbon atoms.
They are reducing sugars.
Examples of monosaccharide are- Glucose, Fructose, Galactose
Glucose
It is the primary substrate in cellular respiration. It provides energy for the metabolic
reactions.
Starch and glycogen are made up of glucose units.

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Alpha glucose (α-glucose)

Here the hydroxyl group on carbon-1 is below the ring.

It is the component of most disaccharides.
Beta glucose (β-glucose)
Here the hydroxyl group on carbon-1 is above the ring.
It is the component of cellulose microfibrils.
Galactose

It is a part of lactose sugar found in mammalian

milk.

Differences between a molecule of alpha-glucose and a molecule of

galactose

In glucose the position of H on carbon 1 is above the

carbon and OH is below the carbon. In galactose it is
reverse
In galactose the position of OH on carbon 4 is above
the carbon and H is below the carbon. In glucose it is
reverse.
Suggest why glucose is soluble in water
Glucose is a polar molecule. It forms hydrogen bonds with water
Fructose
Component of sucrose
It occurs naturally in fruit, honey, and some
vegetables.
It attracts insects and help for seed
dispersal because of its sweetness.

Pentose sugars
. Contain 5 carbons
Examples: Ribose and Deoxyribose

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Disaccharides

Made up of two monosaccharides joined together by

condensation reaction.
Two monosaccharides are joined together by
Glycosidic bond.
This glycosidic bond can be split by Hydrolysis.
The general formula is CnH2n-2On-1
The most important disaccharides are –
Maltose, Sucrose, lactose

Describe how monosaccharides join to form

disaccharide
Monosaccharides joined by condensation reaction by
releasing water molecule and by the formation of
glycosidic bond.

Maltose (malt sugar)glucose + glucose

Formed by the condensation of two alpha glucose molecules joined by 1,4-glycosidic bond.
Can be hydrolyzed to glucose by the enzyme maltase.
Formed by the action of amylase on starch.
It is an intermediate product of starch hydrolysis in plants. It is an essential ingredient in
beer production.
Found in germinating seeds.

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Lactose (milk sugar) (glucose+galactose)

It is the main carbohydrate in milk.

Formed by the condensation reaction of α-glucose and
β-galactose joined by 1,4-glycosidic bond.
It can be hydrolyzed by the enzyme lactase.

Sucrose (glucose+ fructose)

It is the common sugar we use in our

food materials.
It is formed by the condensation
reaction of α-glucose and β-fructose
linked by 1,2-glycosidic bond.
It can be hydrolyzed by the enzyme
sucrase.
It is the form in which sugar is
transported all around the plant.

Distinguish monosaccharides and disaccharides

A monosaccharide consists of one sugar unit whereas a disaccharide consists of two (sugar
units) ;
Disaccharide has a glycosidic bond whereas monosaccharide does not
General formula for a monosaccharide is CnH2nOn
whereas formula for disaccharide is CnH2n-2On-1

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5
Polysaccharides
Formed by the condensation of many monosaccharides joined together by glycosidic bond.
Molecules with 3-10 monosaccharides-Oligosaccharides.
Molecules with more than 11 monosaccharides – Polysaccharides.
These are ideal for storing carbohydrates in cells.
They may be either linear or highly branched.
Three main types of polysaccharides

Starch, cellulose and glycogen are the three

main types of polysaccharides in food.
Starch and glycogen- storage polysaccharide.
Starch – storage carbohydrate in plants.
Glycogen – storage carbohydrate in animals.
Cellulose – structural polysaccharide.

Structure of starch
It is a polymer of α glucose. Alpha glucose monomers
joined by glycosidic bonds. It contains two polymers-
amylose and amylopectin
Amylose is straight chain which is spiralled to form a
helix. Here 1,4-glcosidic bond joins alpha glucose monomers. Amylopectin is branched. It has
1-4 and 1- 6 (glycosidic) bonds. It is a compact molecule.
Amylose

It contains about 200 to 5000

glucose molecules.
Chain of α-glucose molecule joined
by 1,4-glycosidic bond.
This chain turns to helix due to the
presence of hydrogen bond which
holds iodine when we test for starch.
Amylose releases energy slowly.

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 Amylopectin: Contains more than
1000 monomers. It is a branched
structure with both 1,4 and 1,6-
glycosidic bonds.
Branches arise after every 20-30
glucose residues.It can be Hydrolyzed
to release energy quickly by
respiration because of the presence
of branches.
Amylose and amylopectin

Amylose is straight chained / unbranched /

whereas amylopectin is branched ;
Amylose coiled whereas amylopectin is not
Amylose has 1-4 glycosidic bonds whereas
amylopectin has 1-4 and 1-6 glycosidic bonds ;

Bread tastes sweet after chewing for a long period of time.

Digestion of starch produces monosaccharide, glucose that tastes sweet.

Glycogen
Referred to as animal starch.
Only carbohydrate energy store in animals (liver, muscle) .
Made up of many glucose units and are branched.
Branches arise after every 8-10 glucose residues.
Branches are formed due to the presence of 1,6-glycosidic bond.
Unbranched chain contains 1,4-glycosidic bond.
Very compact molecule having many side branches.
Can be hydrolyzed easily.

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Describe the structure of glycogen and explain why it is a suitable molecule for storing
energy.
Consists of α glucose.
Glucose molecules are joined by 1,4 / 1,6 glycosidic bonds
It is a branched structure so it can be hydrolysed rapidly to provide glucose for respiration to
provide energy quickly.
As it is compact more glucose can be stored in a smaller space in a cell.
It has low solubility, so it has no osmotic effect and does not diffuse out of cells
Amylose and glycogen

Amylose is coiled glycogen is not coiled

Amylose has only 1,4 glycosidic bonds
glycogen has 1,4 and 1,6 glycosidic bonds

Differences between a monosaccharide and a polysaccharide

Difference between the structure of lactose and the structure of starch

Lactose is a disaccharide, starch is polysaccharide

Starch is composed of glucose only, lactose is composed of
Glucose and galactose ;
Starch has 1,4 and 1,6 glycosidic bonds, lactose has only 1,4
Glycosidic bonds
Starchy carbohydrate foods are so good during sports!
It is due to the combination of amylose and amylopectin in starch.
Amylopectin release glucose very rapidly when needed.
Amylose releases it more slowly over a long period.

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LIPIDS

SPECIFICATION
(i) know how a triglyceride is synthesised by the formation of ester bonds during
condensation reactions between glycerol and three fatty acids
(ii) know the differences between saturated and unsaturated lipids.
A polymer is a long molecule made up of many identical or similar monomers. Lipids are
made up of non-identical units. So, it is not a polymer

Organic compounds containing carbon, hydrogen and oxygen.

Have lower proportion of oxygen than carbohydrates.
These occur in living things as oil (plant)and fat (animal).
They are soluble in organic solvents like alcohol, benzene etc.
They are hydrophobic molecule.
Supply more energy than that of carbohydrates.
Fats and oils

Lipids which are liquid at room temperature are oils and that of
solid at room temperature are fats.
These are compounds called triglycerides.
These are formed by the condensation reaction of three fatty acid
molecules and one glycerol.
The bond formed between fatty acid and glycerol is ester bond.
Triglycerides

These are formed by the condensation reaction of three fatty acid molecules and one
glycerol. The bond formed between fatty acid and glycerol is ester bond. During the
formation of triglycerides three water molecules are released
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How triglycerides are transported in the blood
Triglycerides are insoluble (in water)
Transported as lipoproteins / as LDL / as HDL
Formed into vesicles
Fatty acid

Saturated fatty acid

Contain the maximum number of hydrogen atoms on

carbon atom.
Hydrogen to carbon ratio is larger.
Hydrocarbon chain is long and straight.
No carbon - carbon double bonds and no more
hydrogen can be added to it.
Single covalent bond is present between carbon
atoms.
Hydrocarbon tail of the fatty acid chain is linear, and
they are packed tightly together.
So, the intermolecular force of attraction is greater.
More energy is needed to separate the fatty acid
chain molecules. Hence, they have high melting point. Results in fats at room temperature
Unsaturated fatty acid

One or two double bonds present between carbon atoms in

fatty acid chain.
One double bond- monounsaturated fatty acid (olive oil)
More than one double bonds- polyunsaturated fatty acid
(vegetable oil, nuts)
A kink or bend is present in the hydrocarbon chain.
As the fatty acid chain is less linear, fatty acids do not pack
closely together.
Intermolecular forces are weaker. So, less energy needed to
separate fatty acid chain molecules resulting in low melting point. They have lesser number
of hydrogen atoms on each carbon than saturated fatty acids.
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How the structure of a saturated lipid differs from that of an unsaturated lipid.
Carbon – carbon double bond present in
unsaturated lipid OR
Saturated lipid has only single bonds
between carbons ;
Hydrogen to carbon ratio is larger in
saturated lipid OR more number of
hydrogen on each carbon
Unsaturated FA chain is bent / saturated
FA chain is straight ;

Saturated and unsaturated fatty acids have different melting temperatures.

The greater the number of double bonds the lower the

melting temperature;
As the fatty acid chain is less linear, fatty acids do not pack
closely together;
Intermolecular forces are weaker.
So, less energy needed to separate fatty acid chain
molecules.

Phospholipid

Esters of fatty acids and glycerol.

One of the fatty acid tails is replaced
by polar group associated with a
phosphate molecule.
It consists of a phosphate head and
two hydrocarbon tails.

Glycolipids :- lipids associated with carbohydrates.

-Found in the cell membrane.
-marker for cellular recognition.
Cholesterol:- belongs to a group called steroids.

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Component of animal cell membrane
-strongly hydrophobic.
take refuge between the tails of phospholipids
Terpenes:- organic compounds with strong smelling.
-Produced by plants mainly conifers and some insects like termites.
Waxes:- esters of fatty acids and alcohols.
Products of hydrolysis of the lipids.
Fatty acid
Glycerol
Monoglyceride / diglyceride

Functions of lipids.

Energy source: hydrocarbon chains are rich

in energy.It stores twice as much energy
than polysaccharides.
(Lipids yield 9 kcal of energy per gram while
carbohydrates and proteins yield only 4 kcal
of energy per gram.)
Insulation: fats stored in the adipose tissue under the skin prevents loss of heat. (blubber in
whale).
Water proofing:

cuticle on leaf epidermis and fruits prevent water loss.

Waxes on skin, fur and feathers of vertebrates prevent
desiccation.

Cell membrane: phospholipids are the major component of cell membrane.

Vitamins: fat soluble vitamins can be absorbed only after dissolving in fat.
Commercial use:
Oil present in the seeds
Honey comb of bees is made of wax.

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 Oxidation of fat produce water. This water is useful in desert
animals like kangaroo rats.

Protection: protects vital internal organs from physical

damage.
Buoyancy: because of less density than water it aid
buoyancy. (aquatic vertebrates like seals)

PROTEINS
Large molecules
Made up of chains of amino acids
Are found in every cell in the body
Are involved in most of the body’s functions and life
processes. The sequence of amino acids is
determined by DNA
Amino acid

All amino acids contain an amine group, –NH2, a

carboxylic acid group, –COOH, and a hydrogen, –
H, attached to a central carbon atom. Each type
of amino acid has a different side chain, called a
residual or R group.

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Peptide Bonds Link Amino Acids/ Describe how amino acids join together to form
proteins

A dipeptide is formed when the acid group

(COOH) of one amino acid joins with the
amine group (NH2) of a second amino acid
through condensation and joins by peptide
bond
Broken down through hydrolysis

Structure of the Protein

Primary structure (Amino acid sequence)↓

Secondary structure (α-helix, β-sheet) ↓
Tertiary structure （Three-dimensional structure formed by assembly of secondary
structures）
↓
Quaternary structure （Structure formed by more than one polypeptide chains）

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 Primary structure is the sequence of amino
acids in a polypeptide joined by peptide
bonds ;

Secondary structure of protein

The two very important secondary structures of proteins are:
a-helix
b-pleated sheet
Both depend on hydrogen bonding between the amide H and the carbonyl O further down
the chain or on a parallel chain.

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Alpha helix
Three-dimensional arrangement of amino acids with the polypeptide
chain in a corkscrew shape
Held by H bonds between the H of –N-H group and the –O of C=O of the
fourth amino acid along the chain
Looks like a coiled “telephone cord”
Beta pleated sheet
Polypeptide chains are arranged side by side.
Hydrogen bonds form between chains
R groups extend above and below the sheet
Typical of fibrous proteins such as silk
Three dimensional structures of proteins

Determined by folding of the chains to form tertiary

and quaternary structure
Tertiary structure is maintained by
Hydrogen bonds
Ionic bonds between ionized R groups
Disulphide bridges
Polar interactions (hydrophilic and hydrophobic)

Quaternary structure
Two or more polypeptide chains held together
Haemoglobin and Insulin

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Albumin is a soluble protein.
Describe how this property is related to the primary structure of albumin.
Primary structure is the sequence of amino acids ;
This determines the folding of the protein/secondary structure
This determines the position / type of bonds (between r groups) which intern determines
the 3 d shape/tertiary structure of the albumin / albumin is a globular protein ;
So that hydrophilic R groups / amino acids are on the outside of the protein/hydrophobic R
groups are inside.

Describe how amino acids join together to form the three-dimensional structure of a
protein.
Amino acids join together by forming peptide bonds between amino group (of one amino
acid) and carboxyl group (of another)
This sequence of amino acids is the primary structure of the protein
This folding (of primary structure) is held together by bonds such as disulfide bridges
/hydrogen bonds / ionic bonds / Van der Waals forces between the R groups.
Liver cells synthesise the protein alpha-1-antitrypsin. This protein is secreted into the blood.
Describe how the primary structure of alpha-antitrypsin results in a protein with a
three-dimensional structure
Primary structure is the sequence of amino acids;
Each amino acid has different R groups and bonds such as hydrogen bond / disulphide bonds
form between R groups
This bonding determines the folding of the polypeptide;
Explain how a change of one amino acid can lead to a change in the structure and
properties of the haemoglobin protein.(Haemoglobin is a protein found in red blood
cells that helps transport oxygen in the blood.)
A change in one amino acid leads to change in primary structure;
This changes the R group, leading to different position and type of bonds like ionic, hydrogen
and disulfide
This results in different {folding / secondary / tertiary / 3D structure /globular}
So, haemoglobin cannot bind with oxygen.

Simple protein
Contains only amino acid
Albumin , globulin
Conjugated proteins
Complex compounds containing globular proteins and tightly
bound non protein material. Glycoprotein, lipoprotein, Hb

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Denaturing

Alteration of the protein’s shape and thus functions through

the use of Heat, Acids, Bases, Salts or Mechanical agitation.
Primary structure is unchanged by denaturing

Fibrous protein

Fibrous proteins are long / contain many amino acids and

it has repetitive amino acid sequence. They have limited
folding. Polypeptides lie parallel to each other and
hydrogen bonds link these chains together.

Structure of collagen

Collagen is a fibrous protein (tendons, ligaments, bones, skin).

Most common structural protein found in animals.
Collagen fibres have a very high tensile strength.
It has a quaternary structure with three polypeptide chains.
The primary structure of these chains is repeating sequences of glycine with other two amino
acids (proline and hydroxyproline).
Glycine has small R group. This allows twisting of polypeptide chain
These three polypeptide alpha chains are arranged in triple helix.
This triple helix is held together by a very large number of hydrogen bonds.
Collagen molecules are found together in fibrils and fibrils held together to form collagen
fibres.
There is no hydrophilic R group on the outside of molecule

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Globular proteins

The polypeptide chain is folded into a compact spherical shape.

These proteins are soluble (due to the hydrophilic side chains that
project from the outside of the molecules
The three-dimensional shapes of globular proteins are critical to
their roles in binding to other substances.
Examples include transport proteins
Structure of haemoglobin

Haemoglobin is a globular
protein
It has four polypeptide
chains which are connected
by disulfide bonds.
Each polypeptide chain
surrounds an iron containing
haem group.
The iron enables
haemoglobin to bind and
release oxygen molecules

Haemoglobin contains a prosthetic group known as haem.

Collagen does not contain a prosthetic group.
Describe three other ways in which the structure of haemoglobin differs from that of
collagen.

Haemoglobin is globular;
In haemoglobin hydrophobic (R) groups on inside / hydrophilic (R) groups on outside ;
Haemoglobin has four polypeptides ;
Subunits are (two) different types
Proportion of glycine similar to that, of other amino acids / in other proteins ;
Wide(r) range of amino acids

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20
The Cardiovascular System:
Blood Vessels
 Pumping of blood around the body.
Help to transport nutrients, hormones, water
and metabolic waste products.
This system include heart, blood and blood
vessels.

Circulatory system is needed to Overcome the limitations

of diffusion.
Also help in transport
Size of the organism and circulatory system
Large animals- need circulatory system
Size of the organism get bigger- SA to Volume ratio gets
smaller.
High diffusion distance.
Exchange of material with the surrounding is difficult
through diffusion.
High metabolic activity
So it need a circulatory system.
Smaller organism- no need of circulatory system

Size of the organism get smaller- SA to Volume ratio get

bigger.

Low diffusion distance.

Exchange of materials with the surrounding occurs very

easily.
Low metabolic activity

Well developed circulatory system is not needed.

Why animals need a heart and circulatory system.

Animals have a small surface area to volume ratio

Diffusion alone is not sufficient

Heart is needed to pump blood around the body

Blood help in mass flow

Transport of oxygen and nutrients

Animals have a high metabolic rate.

6:1 / 6.04:1 ;
Multi-cellular animals require a respiratory system
and a circulatory system.

Diffusion over external surface is not enough as SA to

volume ratio is small.

Respiratory system has a large SA

Diffusion would be too slow over distance

Circulatory system is needed to distribute oxygen to all

parts of the animal
Types of circulatory system
Open circulation:- blood is pumped out by a long tubular
heart into spaces in the body cavity called sinuses.
These cavities are surrounding the organs.
Diffusion between cells and the blood occurs to
exchange materials.
Blood is under low pressure.

Examples
❖ low metabolic rate
Insects ❖ Large surface area to volume ratio
invertebrates ❖ All cells are close to the heart
Circulation in insects do not need blood
vessels…. Why….

• Large surface area to volume ratios

• All the cells are very close to the blood

• Diffusion is fast enough for the exchange of nutrients, gases and

waste

• Rate of metabolism is low

• movement of blood back into the heart is fast enough to return blood

back into the heart

Closed circulatory system
Closed circulation:-
blood is enclosed within tubes called blood vessels.
The heart pumps blood into large vessels
that branch into smaller ones leading into the organs.
Blood is at high pressure

Example : vertebrates
Single circulation:-

Blood passes once through the heart in one

complete circulation.

Example Fish
Circulation in fish

• Circulation in fish is single circulation.

• Blood flows from heart to gills .

• Blood flows from gills to rest of the body.

• Blood flows from body back to heart.

• Blood flows only once through the heart in one

circulation.
Double circulation

Blood passes twice through the heart in one complete

circulation.
Deoxygenated blood from the right ventricle send to
the lungs.
Oxygenated blood from the lungs returns back to the
heart.
Heart pump the blood to the whole body.
Double circulation
Pulmonary circulation:
Blood from the heart send to the lungs for
purification and returns purified blood back to
the heart.

Systemic circulation:
Pure blood from the heart is transported to the
cells of the body and deoxygenated blood
back to the heart.
Importance of double circulation

Blood flows faster and at higher pressure to the body.

Blood flows slower and at lower pressure to the lung.

This reduces risk of damage to lungs.

Helps in more efficient exchange of gases .

Coronary circulation
Aorta →coronary artery→ capillary→ Veins →
coronary sinus → RA

Circulation of the blood in the blood vessels of heart

muscle.
Coronary artery branching from aorta supplies blood to
the myocardium.
Deoxygenated blood is
removed by cardiac veins.
Double circulation enables mammals to carry out
effective gas exchange how…….

One side of heart transports blood to the lungs and other to

the body ;
Separate oxygenated and deoxygenated blood
This maintains a concentration gradient
Lower blood pressure to lungs, higher to body.
Mass flow maximise the supply of O2 to body cells.
Mammals need a good supply of oxygen as they have high
rate of metabolism.
Circulatory system in mammals enables efficient gas
exchange
Mass flow generated by heart ;
Moving blood helps to maintain a concentration gradient ;
A steep concentration gradient gives a fast rate of
diffusion ;
Network of capillaries provide large surface area
Large surface area increases the rate of diffusion ;
capillaries have very thin walls so diffusion is fastest over
small distances ;
No organs / cells / tissues are far away from blood.
Double circulation helps to maintain steep concentration
gradient.
Structure of mammalian heart
• Hollow, muscular organ,
slightly tilted towards the left.

• found in chest between lungs

• 300 grams (size of a fist)

• 4 chambers

• surrounded by membrane called

Pericardium

• Pericardial space is fluid-filled to nourish

and protect the heart. (pericardial fluid)
 The wall of the heart consists of mainly three layers-

outer epicardium-flattened epithelial cells and

connective tissue.

middle myocardium- cardiac muscle cells.

inner endocardium- flattened epithelial cells and

connective tissues.
Chambers of the heart
Upper two chambers – atria (auricles)
Lower two chambers- ventricles.

Atria- receiving chambers

Left atrium- receives oxygenated blood from the Lungs
Right atrium- receives deoxygenated blood from vena cava

Ventricles- pumping blood

Left ventricle- pumps blood to all the organs
Right ventricle-pumps blood to the lungs
Blood vessels
Superior vena cava- receives impure blood from the head, neck, arms and chest
and empty it into right atrium.

Inferior vena cava- collects impure blood from the lower parts of the body and
empty it into right atrium.

Pulmonary artery- deoxygenated blood from right ventricle to the lungs

Pulmonary vein – oxygenated blood from the lungs to the left atrium.

Aorta –oxygenated blood from the left ventricle to the whole body.

Coronary artery- blood to cardiac muscles

Valves
The main valves in the heart and in the blood vessels in
the heart are:
atrio- ventricular valves and semi lunar valves
Atrio- ventricular valves- bicuspid and tricuspid valves
Prevent the back flow of blood from the ventricle to the
atrium during ventricular systole
Bicuspid valve (mitral valve)- present between the left
atrium and ventricle.
Tricuspid valve- present between the right atrium and
ventricle.
Valves
Semilunar valves- present in the pulmonary artery and
aorta.
Separates the ventricle from pulmonary artery and
aorta.
Prevent the back flow of blood from the pulmonary
artery and aorta to the ventricle during diastole.
Role of the heart valves in the cardiac cycle.
During atrial systole ;
Atrioventricular valves open so blood flows from atria to
ventricles ;
During ventricular systole ;
Atrioventricular valve closes to prevent backflow of blood
into atria ;
Semilunar valves open so blood enters into pulmonary
artery and aorta.
During ventricular diastole ;
Semi lunar valves close ;
To prevent backflow of blood from the aorta or pulmonary
artery to the ventricle.
Faulty atrio ventricular valve leads to breathlessness
and lack of energy.

Valve does not shut properly

Some backflow of blood from ventricle to Atrium
during ventricular systole
Lower blood pressure
Less efficient supply of oxygen
Blood pressure in lungs increases
Other structures

Chordae tendineae (tendons)- prevent the valves

from turning inside out during ventricular systole.

Papillary muscles- maintains the tension on the

chordae tendineae.

Septum- separates the right and left sides of the heart.

Prevent the mixing up of oxygenated and
deoxygenated blood.
MAMMALIAN HEART STRUCTURE
there are four chambers ;
position of atria and ventricles ;
left and right sides separate / septum
muscular nature of walls Cardiac muscle ;
relative thickness of ventricle (walls)
position of atrioventricular valves
position of semilunar valves ;
position of tendons / papillary muscles
position of aorta / pulmonary artery
position of vena cava / pulmonary vein
coronary arteries ;
SAN / Sino Atrial Node /pacemaker/ AVN /Atrioventricular Node /
Purkinje fibres /Purkyne fibres / Bundle of His
Difference in thickness of ventricular wall

Wall of the left ventricle is thicker- it has to pump

blood all around the body even to the head against
gravity. So it has to exert high pressure.

Right ventricle- exert a lower pressure to pump the

blood.
Lungs are closer to the heart and its tissues are very
delicate.
High pressure may leads to pulmonary oedema (lungs
fill with tissue fluid)
Why a mammalian heart is divided into a right side
and a left side.

It keeps oxygenated and deoxygenated blood separate ;

This results in as much oxygen as possible being

carried to the tissues

Maintain different pressures in each side

So that blood is pumped into the lungs at low pressure

and to the rest body parts with high pressure.
Hole in the septum

Oxygen rich and oxygen depleted blood mix

Less blood pumped around body

OR

Blood pumped to lungs has a higher oxygen concentration

so less efficient gas exchange

Systemic blood pressure will be low

CARDIAC CYCLE

The rhythmic contraction and relaxation of the heart.

Contraction of the heart- systole- - atrial systole,
-ventricular systole
Relaxation of the heart- diastole.
Atrial systole
Atria fill with blood from pulmonary vein and vena cava.
Pressure in atria increases.
AV valves open.
Blood begins to leak into ventricles.
Semilunar valves remain closed.
Ventricular systole (0.3 sec)
Contraction of ventricular muscle.
Pressure increases than in atria.
AV valves close.
Pressure increases in ventricles than in the pulmonary
artery and aorta.
Semilunar valves open.
Pushes blood into blood vessels.

Volume of blood pumped out by left ventricle is

stroke volume
Stroke volume in one minute is cardiac output
Atrio ventricular diastole (0.4 sec)

Heart refills with blood after contraction.

Elastic recoiling of the heart muscle occurs.
Pressure in both atria and ventricles decreases.
Semilunar valves will be closed.
Atria starts to collect blood from
vena cava and Pulmonary veins
Pressure change in the left side of the heart
Pressure change in the left side of the heart
Ventricular pressure > aortic
pressure

Aortic pressure>ventricular pressure

Pressure change in the left side of the heart

In the initial stage of the ventricular systole pressure is high in the

aorta than ventricle.

At this stage semilunar valve remains closed.

As the ventricular systole continues pressure increases in the

ventricle than in the aorta

At this stage semilunar valve opens.

After pumping all the blood into the aorta, again pressure decreases
in the ventricle and the semilunar valve closes.
During this cardiac cycle, the changes in pressure
that occur in the left atrium and in the left ventricle
are different

Pressure changes are smaller in the atrium than the ventricle

The atrium has less cardiac muscle than the ventricle ;

The atrium does not have to push the blood as far as the ventricle has
to
The increase in pressure happens in the atrium before the ventricle

Atrial systole has to happen before ventricular systole in order for the
ventricle to fill with blood ;

Increase in atrial pressure causes AV valves to open and increase in

pressure in ventricles ;
Finding out heart rate

1. (time for complete cardiac cycle) = 0.96 to 0.98 (sec) ;

2. 60 ÷ cycle time ;
3. correct answer {beats per minute / bpm} ;
Coordination of cardiac cycle

Myogenic stimulation
Stimulation for the heart beat originate in the cardiac
muscle.
There is no nerves but nerve endings from autonomous
nervous system are there.
Heart rate can be controlled by
hormones or nervous system.
 Wave of excitation for the heart beat
originate in the Sino Atrial Node (SAN) or pacemaker.
Spreads through the wall of atria.
Atrial systole occurs.
Wave of excitation is received by Atrio Ventricular Node
(AVN).
The impulse from the AVN is received by Bundle of His.
Impulse is passed on to the walls of the ventricle by
Purkinje Fibres or Purkyne Fibres.
Ventricle starts to contract from the apex of the heart
Presence of non conducting layer (atrio ventricular
septum) between SAN and AVN prevent the direct
transmission of impulse to AVN from SAN.

There is a time delay between atrial systole and

ventricular systole
Practice question
The cardiac cycle consists of three stages: atrial systole,
ventricular systole and ......................................
During atrial systole, the
........................................................ contract and the
................................................................are relaxed. The
...................................................................... valves are
open.
During ventricular systole, the
.................................................. open as oxygenated blood
is forced out of the heart through the aorta to the body and
through the pulmonary
..........................................................to the lungs.
Blood vessels
ARTERIES

❖ Thick walls with smooth elastic fibres.

❖ Elastic fibres help to stretch and recoil.
❖ Smooth muscle helps to constrict and dilate
❖ Collagen provides flexibility.
❖ Small lumen.
❖ No valves except in the heart.
❖ Blood at high pressure.
❖ Carry blood from the heart to tissues.
ARTERY-STRUCTURE RELATED TO FUNCTION
Wide wall help to withstand blood under high pressure
Narrow lumen to maintain high pressure ;
Presence of elastic fibres- it allow vessel to stretch to
accommodate high pressure and recoil to maintains
pressure
Smooth muscle contracts to squeeze blood along;
Smooth lining reduces friction ;
Folded lining allow artery to stretch.
AORTA- STRUCTURE RELATED TO FUNCTION

• There is a thick wall to avoid rupture and to withstand high

pressure.
• Elastic fibres to maintain blood pressure by elastic recoil.
• Smooth endothelial wall to reduce friction .
• Semi lunar valve present to prevent back flow during
diastole.
• Large lumen to accommodate large volumes of blood .
• Branches to supply blood to different parts of the body
including coronary arteries.
VEINS
❖ Thin walls with collagen and less elastic.

❖ Large lumen.

❖ Many valves.

❖ Blood at low pressure.

❖ Volume of blood is high.

❖ Carry deoxygenated blood from tissues to the heart.

VEIN- STRUCTURE TO FUNCTION
o Thin walls – blood flow at low pressure
o Little smooth muscle or elastic fiber – no stretching
and recoiling
o Wide lumen – Allow large volume of blood to flow
(blood reserve)
o Valves present – prevents back flow of blood
Artery and vein
Artery Vein
Small lumen Wide lumen
No valves Valves present
Thick tunica media Thin tunica media
More elastic fibres Less elastic fibres
More collagen less collagen
CAPILLARY
Link between arteries and veins.

Wall is very thin, one cell thick and permeable and contain
pores.

Lumen is very small.

Valves are not present.

Blood is at low pressure.

Exchange materials between blood and tissues.

Blood changes from oxygenated to deoxygenated.

CAPILLARY- STRUCTURE RELATED TO FUNCTION

Thin walls with one layer of cells

So short diffusion distance

Gaps/pores between cells

Allows exchange of materials

CAPILLARY AND VEIN

Capillary walls are one layer of cells .

No elastic tissue in the capillary walls.
No collagen in capillary
No valves in capillaries .
Capillaries have a very narrow lumen.
Capillaries have pores;
Difference between artery and capillary
ARTERY CAPILLARY

Thick wall Thin wall

Lots of collagen No collagen

Lots of muscle No muscle

Lots of elastic tissue No elastic tissue

No pores Pores present

Narrow lumen Narrower lumen

Semilunar valves and elastic fibres in aorta-
Location and function

Semilunar valve
Location :base of aorta
Function : prevents backflow of blood into ventricles
during diastole
Elastic fibres
Location : tunica media
Function : allows stretching to prevent damage of the
aorta and recoil to maintain the pressure of the blood
Blood flow through the vein
1

Blood is at low pressure in veins.

Contraction of the skeletal

muscles help to squeeze the blood
forward by opening the valves.

Suction force – reduced blood

pressure in the thoracic cavity
because of breathing movements
Pressure change in blood vessels
Pressure change in blood vessel
2

High blood pressure is in the aorta.

Decline through out the length.
Steepest change is in arterioles.
The most decrease in Blood pressure is in arterioles
because of high resistance.
Low pressure in arterioles protect the capillaries from
getting damage.
There is no smooth muscles and elastic tissues in veins.
Large lumen and high volume of blood decrease the BP in
veins.
Capillaries- large surface area decrease the blood pressure.
Tissue fluid formation
Tissue fluid formation 3

High hydrostatic pressure in the arterial end.

Ultra filtration of water and solute particles like glucose and proteins
occurs.
The fluid surrounding the body cells- tissue fluid or interstitial fluid.
Exchange of materials occurs between body cells and tissue fluid by
diffusion.
85% of tissue fluid is getting back into the venous end of the
capillary by osmosis which contains impurities.
15% is entering into the lymph vessel.
Lymph vessel pour that into the veins and finally into the heart.
Blood and tissue fluid 4

Blood contains more proteins than tissue fluid.

Plasma protein is large molecule and it cannot pass

through the pores of capillary.

Blood is present in the blood vessels but tissue

fluid is around the cells.

Blood contain RBCs but tissue fluid does not.

Blood clotting
Blood clotting 5

There is a cascade of events leading to blood clotting

Platelets get activated and accumulate in the damaged site
Platelets release thromboplastin
In the presence of calcium ions and vitamin K
thromboplastin convert prothrombin into thrombin ;
Thrombin acts as an enzyme
This convert soluble fibrinogen into insoluble fibrin ;
Fibrin form a mesh
Trap platelets / blood cells in the mesh form blood clot
Importance of blood clotting 6

Provides frame work for cellular or tissue

repair.
Clot prevent further bleeding.
It prevent the entry of pathogens into the
body.
Differences between fibrinogen and fibrin

Fibrinogen is globular and fibrin is fibrous ;

Fibrinogen is soluble and fibrin is insoluble

Fibrinogen contains more amino acids than fibrin

ATHEROSCLEROSIS
Atherosclerosis
Hardening and narrowing of artery because of the
deposition of atherosclerotic plaque.

As the disease progress, it reduce the flow of

oxygen and blood.

Increases the risk of cardio vascular diseases.

Risk factors of atherosclerosis 7

High blood pressure

Smoking
High cholesterol level in the blood (LDL)
Obesity
Lack of exercise
Poor diet
Gender
How atherosclerosis develops 8

Damage to endothelial cells lining artery wall

Stimulate inflammatory response
White blood cells accumulate in the damaged area
Build up of cholesterol in damaged area
Calcium salts also accumulate
This form a plaque / atheroma
Artery loss its elasticity and lumen become narrow
This process is self–perpetuating
Consequence of atheroma 9

Atheroma continue growing.

Thickens the arterial wall.
Arterial wall become less elastic.
Plaque bulge into the lumen and makes the lumen
smaller.
Increases the BP.
More damage occur and leads to more plaque
formation.
This makes BP even higher. (positive feedback)
 10
Formation of blood clot

Platelets start to accumulate in the roughened surface

of atheroma.
Trigger clot formation.
The blood clot within the blood vessel is called
thrombus.
Thrombus may detach from the place and circulate in
the blood stream- embolus
Moving of embolus in the circulatory system and
causes blockage- embolism
Consequences of atherosclerosis 11

Cardio vascular disease - angina

Cerebro vascular disease -stroke

Peripheral arterial disease-

Aneurysm
Arrhythmia
Life style diseases
Non-transmissible diseases are influenced by the sort
of life we lead.
Cardio vascular disease 12

Atheroma in the coronary artery.

Blocks blood supply to the cardiac muscle.
Cardiac muscle deprived of oxygen and nutrients
(Ischaemia).-
Ischaemia- local anaemia in a given body part because of
thrombosis or embolism.
Lack of blood supply leads to death of tissue- necrosis
Anaerobic respiration leads to the accumulation of lactic
acid.
This leads to pain called angina (angina pectoris) and heart
attack (myocardial infarction).
Angina pectoris 13

o Narrowed coronary arteries fail to deliver sufficient

oxygen to cardiac muscles
o Leads to anaerobic respiration
o Causes a gripping pain in the chest
o Pain starts with exercise and goes when resting
How a blood clot can cause a heart attack 14

Prevents oxygen reaching the heart muscle

Prevents aerobic respiration
Cardiac muscle is unable to contract / dies
Size and position of block in coronary artery 15

The area of dead heart muscle will be downstream of the

atheroma
Each artery supplies cells with oxygen / glucose
Cells supplied by the blocked vessel will die due to lack of
energy /respiration
If the atheroma is located near the end of an artery / in a
small artery then the area of dead muscle will be small ;
Pulmonary thrombosis, reduce gas exchange
in the lungs. 16

Reduces the flow of blood to the lungs

Decreases the concentration gradient and diffusion rate
How it affect heart function and other body
cells 17
Effect on heart:
less blood flow (through the coronary artery) to cardiac / heart muscle /muscle cells
heart muscle / cells dies / does not work as effectively
may cause a heart attack / angina
less forceful contraction
Effect on rest of body:
less blood flows/ blood flow slower to body cells
/organs
lactic acid builds up / more likely to get cramp fatigue / tiring easily
less oxygen in the blood
Effect on heart cells and / or body cells
less oxygen
less glucose
less aerobic respiration
less energy released
body cells start /
increase anaerobic respiration
less waste products removed
Cerebro vascular disease 18

Blood clot in the artery supplying blood to the

brain.
Leads to the deficiency of blood flow which leads
to loss of brain function and to stroke.
Two types of stroke- haemorrhagic and ischaemic
stroke.
A blood clot in an artery leading to the brain could
cause a stroke 19

Reduced blood flow

Less oxygen /glucose reaches brain
Less aerobic respiration
less ATP produced
Brain needs lots of energy / ATP to function
Lactic acid produced from anaerobic respiration
Lactic acid inhibits enzymes
Symptoms of stroke 20

dizziness
Numbness
Confusion
Slurred speech
Blurred vision
Loss of balance
Drooping of mouth and eyes on one side
Arm weakness
Paralysis
Arrhythmia 22

Coronary thrombosis leads to obstruction of blood

flow.
Cardiac muscle downstream from the obstruction may
die.
Damage may occur in the cardiac muscle region which
conducts impulse for heart beat.
Malfunction in the conduction of impulse for heart
beat.
Leads to irregular heart beat. (arrhythmia)
Aneurysm 21

Tear in the wall of artery due to atherosclerosis.

Blood enter the muscles and build up behind the
blockage.
Leads to balloon like swelling in the artery. (aneurysm)
Weaken the wall of blood vessel
Leads to internal bleeding (haemorrhage)
• The first oxygen molecule that binds to the haemoglobin
changes the arrangement of the molecule.
• This makes it easier for the following oxygen molecules to
bind.
• The final oxygen molecule binds several hundred times
faster than the first.
• When oxygen dissociates from haemoglobin it gets
progressively harder to remove the oxygen.
• In the lungs the concentration of oxygen in the RBC is
relatively low.
• Oxygen moves in to the RBC from the air in the lungs by
diffusion.
• The oxygen is bound to the haemoglobin.
• So the free oxygen concentration the cytoplasm of the RBC
stays low.
• This maintains steep concentration gradient from the air in
the lungs to the RBC.
• So more and more oxygen diffuses in and joins onto the
haemoglobin.
• In the body tissues the oxygen levels are relatively low.
• The concentration of oxygen in the cytoplasm of RBC is
higher than in the surrounding tissue.
• So oxygen diffuses into the body cells.
• The haemoglobin molecules give up some of their oxygen.
• Oxygen saturation of the environment falls in the tissues,
oxygen is released rapidly
The Bohr effect

• The way in which haemoglobin collects and release oxygen is also affected by the
proportion of carbon dioxide in the tissues.
• When the proportion of carbon dioxide in the tissues is high, the affinity of haemoglobin
for oxygen is reduced.
• Haemoglobin needs higher levels of oxygen to become saturated and releases oxygen
much more easily.
• In active tissues with high carbon dioxide levels, haemoglobin releases oxygen more
readily.
• Carbon dioxide levels in the lung capillaries are relatively low, which makes it easier for
oxygen to bind to the haemoglobin.
• The changes in the oxygen dissociation curve that result as the carbon dioxide level
changes are known as Bohr effect
Ans : 10%
(iii) Scientists extracted the genes for mammoth haemoglobin and used
them to produce mammoth haemoglobin.
The oxygen dissociation curve for mammoth haemoglobin at 38 °C was
found to be the same as for the Asian elephant at 38 °C.
Lowering the temperature did not shift the oxygen dissociation curve.
Explain how these observations show that this haemoglobin enabled
mammoths to be adapted for life in cold Arctic regions. (3)

affinity of haemoglobin for oxygen does not change (ACCEPT

haemoglobin does not bind to oxygen tightly when cold /
haemoglobin binds to oxygen more weakly (than elephants) when
cold)

therefore oxygen is still released

therefore heat is still produced by respiration

(ii) When 1g of haemoglobin is fully saturated it
carries 1.3 cm3 of oxygen.
Calculate the volume of oxygen released by 1 g
of haemoglobin to this active muscle tissue.
Show your working. (2)

ECF from part (i)

100% - 10 % = 90%
1.3 – 0.13 = 1.17
(90 ÷ 100) x 1.3 = 1.2 cm3
ALLOW 1.17 cm3
no units or incorrect units gains ONE
mark only
correct response with no working
gains full marks
Northern elephant seals have a high concentration of haemoglobin in their
blood.
The graph shows the oxygen dissociation curves for myoglobin, adult
haemoglobin and fetal haemoglobin.

Which of the rows correctly matches each curve with myoglobin, adult
haemoglobin and fetal haemoglobin?
 TRANSPORT OF OXYGEN AND CARBON DIOXIDE
Learning objective:
Understand the role of haemoglobin in the transport of oxygen and carbon dioxide
Understand the oxygen dissociation curve of haemoglobin, the Bohr effect and the significance of the
oxygen affinity of fetal haemoglobin compared with adult haemoglobin.
TRANSPORT OF OXYGEN
The many haemoglobin molecules that are in the red blood cells transport oxygen. Each haemoglobin
molecule is large globular protein consisting of four peptide chains, each with an iron containing prosthetic
group.

Each group can collect four molecules of oxygen in a

reversible process to form oxyhaemoglobin.
The first oxygen molecule that binds to the
haemoglobin changes the arrangement of the molecule
making it easier for the following oxygen molecules to
bind.
The final oxygen molecule binds several hundred times
faster than the first.
But when oxygen dissociates from haemoglobin, it gets
progressively harder to remove the oxygen.

In the lungs the concentration of oxygen in the RBC is relatively low.

Oxygen moves in to the RBC from the air in the lungs by diffusion.
The oxygen is bound to the haemoglobin.
So, the free oxygen concentration the cytoplasm of the RBC stays low.
This maintains steep concentration gradient from the air in the lungs to the RBC.
So, more and more oxygen diffuse in and joins onto the haemoglobin.
In the body tissues the oxygen levels are relatively low.
The concentration of oxygen in the cytoplasm of RBC is higher than in the surrounding tissue.
So, oxygen diffuses into the body cells.
The haemoglobin molecules give up some of their oxygen.
Oxygen saturation of the environment falls in the tissues, oxygen is released rapidly

Oxygen dissociation curve- it is

the graph showing the
percentage saturation of
haemoglobin with oxygen at
different partial pressures of
oxygen

The structure of haemoglobin causes the oxygen dissociation curve of haemoglobin to be this sigmoidal (S)
shape.
Hemoglobin is composed of four polypeptide chains (sub- units) with haem group.
Binding of the first oxygen molecule is difficult.
Once it binds, the tertiary structure of Hb changes and binding of other molecules become easier.
As hemoglobin becomes saturated, less oxygen can bind and so the curve flattens out

1
Relationship between O2 partial pressure and affinity/ saturation of haemoglobin

There is a positive correlation between these two.

As oxygen partial pressure increases, affinity of
haemoglobin increases.
The correlation is not linear but is curved (produces
sigmoid curve called oxygen dissociation curve, ODC)
Middle portion of ODC has a steep gradient so when
respiring tissues change from resting to active and partial
pressure of O2 falls, there is a large drop in affinity, so
more O2 would be delivered to the respiring tissues.

Fetal haemoglobin and adult haemoglobin

The blood of the fetus contains a special form of the oxygen carrying
pigment called fetal haemoglobin.

Fetal haemoglobin has a higher affinity for oxygen than the adult
haemoglobin of the mother.
Fetal haemoglobin can remove oxygen from the maternal blood even
when the proportion of oxygen is relatively low.
The maternal and fetal blood run in opposite directions.
This makes a steep oxygen concentration gradient between mother’s
blood and her fetus. And maximize the oxygen transfer to the blood
of the fetus.

2
Benefit of fetal haemoglobin having high affinity
So the oxygen will dissociate from the mother’s haemoglobin and associate with the fetal haemoglobin at the
low partial pressures of oxygen in the placenta, so it has enough oxygen for its needs.
Fetal haemoglobin ODC will be to the left of adult hemoglobin.

Why do adults not keep with fetal haemoglobin

Due to the high affinity of fetal haemoglobin less oxygen will be unloaded at the respiring tissues.

Affinity of organisms in low oxygen environment

Organisms have high affinity so curve to the left.

It can readily associate with oxygen at the low partial pressure of oxygen.

Affinity of active organisms

They have low affinity so curve to the right.
More oxygen can be unloaded to meet the cells demand for more respiration.

Affinity of small organisms

Small organisms have large surface are to volume ratio

So, they lose a lot of heat and needs to respire to generate heat.
It has low affinity, curve to the right, so unloads enough oxygen for
the cells demand for more respiration.

Bohr effect

Relationship between CO2 partial pressure and affinity/ saturation of haemoglobin

There is a negative correlation between CO2 partial pressure and

affinity/ saturation of haemoglobin
This occurs at the site of respiring tissues.
The increased carbon dioxide level lowers the pH of the blood, makes
the hemoglobin change shape, so oxygen is released, lowering affinity.
This shifts ODC to the right, called the Bohr shift.
More oxygen will be delivered to the respiring cells.
Higher pH causes hemoglobin to hold onto more oxygen will

The changes in the oxygen dissociation curve that results as the carbo dioxide level changes are known as
Bohr effect

3
 TRANSPORT OF CARBON DIOXIDE

Carbon dioxide diffuses from the respiring cells of the body tissues into the blood along a concentration
gradient.
When carbon dioxide is dissolved in the blood it reacts slowly with water and form carbonic acid, H2CO3
(catalyzed by carbonic anhydrase)
The carbonic acid separates to form hydrogen ions (H+) and hydrogen carbonate ions (HCO3-).
The presence of hydrogen ions in the RBC help to dissociate oxyhemoglobin to release oxygen which will
diffuse into the tissues for respiration.
The HCO3- ions diffuse out of the RBC into the plasma and to balance the electrical potential chloride ions are
shifted to RBC. (chloride shift)
About 5% of the carbon dioxide is carried in solution in the plasma.
10-20% combines with haemoglobin molecules to make carbaminohaemoglobin.
Most of the carbon dioxide is transported in the cytoplasm of the red blood cells as hydrogen carbonate ions.
In the body tissues, there is a high concentration of carbon dioxide in the blood.
So carbonic anhydrase catalyses the formation of carbonic acid.
In the lungs, the carbon dioxide concentration is low.
Carbonic anhydrase catalyses the reverse reaction and free carbon dioxide diffuses out of the blood into the
lungs.

Chloride shift in systemic capillaries

Carbon dioxide is generated by cellular respiration in tissues
This carbon dioxide diffuses from tissue to plasma and then to RBC
In RBC, water and carbon dioxide combine to form carbonic acid
Carbonic acid dissociates to give hydrogen ion (H+) and bicarbonate ion (HCO3-)
Concentration of HCO3- builds up inside RBC
HCO3- diffuses from RBC into plasma and chloride shifts into RBC (chloride shift)
Chloride shift in pulmonary capillaries
HCO3- diffuses into RBC and chloride shifts into plasma
In RBC, bicarbonate ion combines with hydrogen ion released from reduced Hb to form carbonic
acid.
Carbonic acid dissociates to give H2O and CO2.
Carbon dioxide diffuses from RBC to plasma and then to alveola to be exhaled.

4
 RISK FACTORS OF CVD
Cardiovascular disease.
disease of the heart / blood vessels by high blood pressure, atherosclerosis and narrowing of the
lumen which reduces blood supply.
Risk factors associated with CVDs
Gender
Genetic
Age
Diet
High BP
Inactivity
Stress
Obesity
Smoking
Excess alcohol
Age
Major risk factor for CVDs. Risk increases with age in both men and women
Due to age Blood vessels (ARTERY) lose their elasticity, narrowing of artery
and which raises blood pressure.
Gender
Risk is more in men than women
It is less in women due to the presence of female hormone oestrogen,
which reduce the buildup of plaque.
Oestrogen helps to decrease LDL and increases HDL level
Diet
Eat healthy diet
Use vegetable oil- It contains poly unsaturated fatty acids which form HDL
Use lean meat, poultry- Animal fat contain saturated fatty acids which forms LDL. High intake of saturated
fatty acid is linked with high blood cholesterol level. Cholesterol is involved in plaque formation in
atherosclerosis.
Use low fat dairy foods
Eat less fat and fatty foods- Excess fat stored in the adipose tissue leading to obesity

Use more fruits and vegetables- Contains more fibers and antioxidants which neutralize free radicals and
prevents cellular damage mainly myocardial cells

Eat fish at least twice a week

Fish oil contains omega-3 fatty acids which are essential for cell functioning.
Reduces heart diseases and joint inflammation
Use less salt in cooking
Excess salt causes the retention of water in the blood. This increases the volume of blood and blood
pressure.

Why high blood pressure increases the risk of CVD

High blood pressure can cause damage to the endothelial lining of arteries
This leads to inflammatory response and there by formation of plaque / atheroma / atherosclerosis
Lumen becomes narrowed.
This results in cells of heart being deprived of oxygen and nutrient.
Inactivity
Lack of exercise is a major risk of CHD
Exercise leads to vasodilation- decreases BP-reduces atheroma.
Exercise strengthens the heart enabling it to contract more forcefully
Increases the stroke volume
Decreases the heart rate
Exercise increases HDL
Reducing the risk of obesity by maintaining energy input and
output there by plaque formation
Exercise is usually included as part of a weight loss programme
Exercise uses energy
The longer the exercise, the more energy used and more weight loss
When energy input lower than energy output it leads to Weight loss
Exercise increases metabolism / muscles use more energy than fat.
High fat diet and inactivity leads to CVD
Input is greater than output which leads to energy imbalance
So individual become overweight and increases blood pressure
Excess fat in the diet increases blood cholesterol / LDL levels
This causes damage to endothelium and formation of atheroma / plaque / atherosclerosis
Artery wall losses its elasticity and lumen become narrowing.
Reduces oxygen and nutrient supply to cardiac muscle cells.
Stress
Increases blood pressure
Increases the heart rate
Stress increases obesity
Due to obesity heart has to work harder to propel the blood. This increases the strain on the heart and
there by leads to high blood pressure.
Obesity
Risk factor for CHD
Excess fat deposited in the adipose tissue leads to obesity
Body mass index above 30 is considered as obese
Excess fat in the adipose tissue leads to weight gain
It is a risk factor for high BP, high blood cholesterol, diabetes etc
A diet consisting of a high proportion of carbohydrates could lead to obesity.
Carbohydrates provide a source of energy
If energy input is greater than the energy output weight will be gained
Because excess carbohydrate is converted to fat
Excess Alcohol consumption
Moderate drinking of alcohol increases the HDL level
Red wine contains antioxidants which prevents damage to the cells of the heart by neutralizing free
radicals.
Safe intake for men is 3 to 4 units per day, for women 2 to 3 units
Heavy drinking raises blood pressure, leads to obesity, irregular heartbeat, and damages liver cells
Smoking

Obesity indicators
Waist-to –hip ratio and body mass index are the two indicators used to find out whether a person
is obese or not
Body Mass Index (BMI)
It is a quick and easy method for determining whether a person’s weight is appropriate for his or height
It can be assessed by dividing body weight (in kilograms) by height (In meters squared) or kg/m2
Obesity related health problems increase when a person’s BMI exceeds 25
BMI is not a good predictor of CVD of its own.
• It is not appropriate for pregnant women or for use in some medical conditions or with children
• It is also inappropriate for athletes. Most top athletes would have BMIs in the obese range. does not
recognize between fat and muscle.
• It is more difficult to assess obesity in children. Young people grow and their body composition
changes as they mature. (so, both age and gender are important in calculating what is normal until
they become adults).
• BMI values also underestimate body fat in older people who have lost a lot of their muscle mass.

Calculate the body mass index for person with a body mass of 95kg and a height of 1.70 meter. Show
your working
Ans:32.87
Waist-to –hip ratio
Waist-to-hip ratio is used to assess abdominal obesity
Abdominal obesity is a much more significant factor for heart attack than BMI.
There is a correlation between Chronic diseases and fat stored in the mid-section.
It can be measured by dividing the waist measurement by the hip measurement

A ratio above 0.80 for women and 0.95 for men is at risk for a number of diseases

LOW DENSITY LIPOPROTEINS & HIGH DENSITY LIPOPROTEINS

HDLs
Triglyceride from unsaturated fats combine with cholesterol and proteins form HDL
Transport cholesterol from the body tissues to the liver
Have greater proportion of proteins
Reducing the depositing of cholesterol
Exercise tends to increase HDL
Smoking reduces HDL
HDL help to remove cholesterol from the plaque
LDLs
Triglycerides from saturated fats combine with cholesterol and proteins form LDLs
Major cholesterol carriers in the blood
Have lower proportion of proteins
Increases the formation of fatty plaques of atherosclerosis
Excess LDLs overload membrane receptors
Receptors help to remove LDL from the blood
Saturated fats also interfere with LDL receptors and elevates the risk of atheroma formation
Lowering blood cholesterol levels can reduce the risk of CVD.
Less cholesterol in blood to build up on artery wall
Less likely to develop atherosclerosis
So, no chance of narrowing of arteries, ischaemia, decrease in flow of
blood to heart
Antioxidants and heart health
Antioxidants are molecules that inhibit the oxidation of other molecules
which may damage cells
Antioxidants are found in fruits and vegetables.
Vitamin C is important in the formation of connective tissues in the body,
such as in the bones, teeth, skin and many internal body surfaces including
the endothelial lining of the blood vessels.
Lack of vitamin C causes damage to the endothelial lining of the artery
and which can lead to atherosclerosis.

TREATMENT FOR CARDIO VASCULAR DISEASES

Treatments include
life style changes
Medicines
Medical procedures
Surgery
Medicines
Antihypertensives
Angiotensin receptor blockers
ACE inhibitors
Diuretics
Beta blocking drugs
Calcium channel blocking agents

Cholesterol lowering drugs

Statins (HMG CoA reductase inhibitors)

Anticoagulants and Platelet inhibitory drugs

Heparin
Aspirin
Warfarin

Angiotensin receptor blockers

Angiotensin is a hormone which stimulates the constriction of blood vessels
and causes high blood pressure.

Block angiotensin from binding with receptors on the smooth muscles of the
artery prevent vasoconstriction and thereby high BP.

Side effects: Dizziness, Abnormal taste sensation, rash

ACE Inhibitors
ACE inhibitors block the production of angiotensin, which reduces the
constriction of blood vessels and keeps blood pressure lower.
Side effects: Skin rash, Feeling sick or vomiting, Sinusitis

These are sympathetic nerve inhibitors.

Sympathetic nerves stimulate arteries to constrict, which raises blood pressure.
The inhibitors prevent these nerve signalling to the arteries, which helps to keep the arteries dilated and
blood pressure lower.

Diuretics

Diuretics act on kidneys.

This eliminates excess fluids and salts, so that decreases
blood volume.
With less blood smaller volume of blood is pumped from
the heart and the blood pressure falls.
Side effects: Skin rash, Diarrhoea

Beta blocking drugs

Blocks the binding of Adrenaline with beta receptors

Slows the nerve impulses that travel through the heart
Slow down the heart rate and decreases the Blood pressure
Side effects: Fatigue, Dizziness, constipation

Calcium channel blocking Agents

Affects the movement of calcium into the cells of the heart

and the blood vessels
Relax blood vessels
Increase the supply of blood and oxygen to the heart
Side effects: Fluid retention, Headache, Constipation
Cholesterol lowering drugs Statins (HMG C) are a group of drugs that lower the level of
blood cholesterol.
They block the enzyme in the liver that is responsible for
making cholesterol.
They are very effective at blocking the production of LDLs.
It also improves the balance of LDLs and HDLs and reduce the
inflammation in the arterial lining and reduces the risk of
atherosclerosis
Side effects: liver damage, Kidney damage, skin rash, dizziness

Anticoagulants and platelet inhibitory drugs

These are drugs used to prevent the blood clotting too easily.
Anticoagulant (warfarin) interferes with the manufacture of
prothrombin in the body. This prevents blood clotting
Thrombin is formed from prothrombin.
Thrombin acts as the enzyme to convert fibrinogen to fibrin
which trap RBC and form blood clot
Platelet inhibitory drugs (aspirin and clopidogrel) make the
platelets less sticky, and reduce the clotting ability of the blood.
Benefits- anticoagulants
Reduce the ability of the blood to form clots
Stops an existing clot from worsening
Prevent blood clots from forming after the replacement of a heart valve
Reduce the risk of a stroke or a heart attack after a first heart attack
Reduce the chance of blood clot forming during open heart surgery or bypass surgery
Drug urokinase dissolve existing clot
Risks
(internal) bleeding / haemorrhage / stomach ulcers / eq ;
Rashes/ hair loss,
nausea/vomiting,
diarrhoea/ irritation to stomach lining

How anticoagulants can help reduce the effects of CVD.

Anticoagulants prevent the formation of a blood clot either by inhibiting or by preventing the synthesis of
clotting factors
It also reduces the ‘stickiness’ of platelets and prevent them from aggregating
By preventing the blood clot formation, the risk of blood vessels becoming blocked is reduced and blood
can flow normally in arteries.
Surgery
Include balloon angioplasty and coronary artery bypass grafting
Balloon Angioplasty-Procedure to open blocked or narrowed coronary artery
Improve blood flow to the heart, relieve chest pain and prevent heart attack
 CELL MEMBRANE

SPECIFICATION

(i) know the structure and properties of cell membranes

(ii) understand how models such as the fluid mosaic model of membrane structure are interpretations of data
used to develop scientific explanations of the structure and properties of cell membranes.

(iii)understand what is meant by osmosis in terms of the movement of free water molecules through a
partially permeable membrane, down a water potential gradient.

(iv) understand what is meant by passive transport (diffusion, facilitated diffusion), active transport (including
the role of ATP as an immediate source of energy), endocytosis and exocytosis

(v) understand the involvement of carrier and channel proteins in membranetransport

Phospholipids form bilayer on cell membrane

Phospholipids have polar / hydrophilic heads and non-polar / hydrophobic tails

Phosphate head face towards water medium and fatty acid tails face away from the water medium

Gorter and Grendel model

Made up of only phospholipid bilayer.

This bilayer is so weak and it cannot hold all the cell contents.

Davson- Danielli sandwich model

Outer and inner layers of protein coat

Middle phospholipid bilayer

Phospholipid bilayer is sandwiched between two layers of protein.

Drawbacks

According to this

All the membranes are similar in structure

 Membrane proteins would be exposed to hydrophilic environments (not a stable arrangement)

Fluid- mosaic model of Singer and Nicolson

Membrane is made up of phospholipid bilayer and proteins are randomly embedded into this layer.

Fluid- phospholipid molecules can change the places within the membrane.

Proteins and phospholipids can move around in the plasma membrane.

Proteins are scattered in the membrane

Mosaic- proteins are randomly embedded.

FUNCTIONS OF MEMBRANE COMPONENTS

Phospholipid bilayer:- maintain the composition of the cytoplasm and act as a selectively permeable membrane.

Glyco lipid:-carbohydrate attached on phospholipid. Act as receptor site for chemical signals

Glyco protein:- carbohydrate attached on protein, act as name tag (antigens)

Glycocalyx :- (glycolipid+ glycoprotein ) cell recognition, chemical protection and adhesion

Cholesterol:- makes the membrane less fluid and more stable and also reducing the entry and escape of polar
molecules

It combines with fatty acid tails and holds the fatty acid chains together.

This reduces the movement of phospholipid.

At warm temperatures, it restrains the movement of phospholipids and reduces fluidity.

At cool temperatures, it maintains fluidity by preventing tight packing.

Two populations of membrane proteins.

Peripheral proteins are not embedded in the lipid bilayer at all.

Instead, they are loosely bounded to the surface of the protein, often connected to the other population of
membrane proteins
Integral proteins penetrate the hydrophobic core of the lipid bilayer, often completely spanning the membrane
(a transmembrane protein).

Transmembrane proteins

Channel proteins :- selective transport of polar molecules

Carrier proteins :- transport of molecules by facilitated diffusion

Describe the structure of the cell membrane.

Cell membrane is made up of phospholipid bilayer and proteins

Phospholipids have polar / hydrophilic heads and non-polar / hydrophobic tails

Phosphate head face towards water medium and fatty acid tails face away from the water medium

There are different groups of proteins. They are extrinsic, intrinsic, transmembrane proteins

Cell membrane also contains glycoproteins, lipoproteins and cholesterol

Suggest how cholesterol affects membrane fluidity

It combines with fatty acid tails

And holds the fatty acid chains together ;

This reduces the movement of the phospholipid / fatty acid tails

Function of carrier proteins in a cell surface membrane

Involved in facilitated diffusion-movement of { large molecules / polar molecules / ions from a high
concentration to a low concentration

· involved in active transport - needs ATP to move molecules against concentration gradient

Compare the Davson-Danielli model With the fluid mosaic model.

1. Both have a phospholipid bilayer and protein

2. The fluid mosaic model has proteins scattered within the phospholipid layer while the davison – danielli
model has protein layer on the outside of the membrane only

3. Other components present in fluid mosaic model e.G. Glycolipid, glycoprotein, cholesterol

Davson-Danielli model and movement of molecules in fluid mosaic model

1. Molecules would not be able to diffuse through the protein layers .

2. No channels or carrier protein for facilitated diffusion, active transport and osmosis;

3. Fluidity of membrane limits fusion of vesicles for endocytosis and exocytosis

Freeze fracture technique

A special technique, freeze-fracture, splits a membrane along the

middle of the phospholipid bilayer prior to electron microscopy.

This shows protein particles interspersed with a smooth matrix,

supporting the fluid mosaic model.

Supporting fluid mosaic model

TRANSPORT ACROSS CELL MEMBRANE

DIFFUSION

Diffusion is the tendency for molecules of any substance to spread out

into available space.

Movement of molecules from areas of higher concentrations to

lower concentrations.

Small non polar molecules can move through phospholipid bilayer

by simple diffusion
FACILITATED DIFFUSION

Movement of molecules down concentration gradient across the

membrane using either channel protein or carrier protein.

OSMOSIS

OSMOSIS

Osmosis is the net movement of water molecules from

a solution with a lower concentration of solute to a

solution with a higher concentration of solute through

a partially permeable membrane

CELLS IN DIFFERENT SOLUTIONS

ACTIVE TRANSPORT

Movement of molecules occurs against a concentration gradient across the membrane

The substance to be transported binds to the carrier protein.

Energy from ATP changes the shape of carrier protein

The substance is released on the other side of the membrane.

Movement occurs in one direction.

Transport of oxygen and carbon dioxide

Oxygen and carbon dioxide are small and non-polar so it can pass directly through bilayer.

Transport occurs by simple diffusion from a region of high concentration to a region of low concentration.

The movement of potassium ions into a cell

By active transport.

Concentration of potassium ions is higher inside the cell than outside

ATP is used to change the shape of carrier protein.

The movement of glucose into a cell

By Facilitated diffusion through a channel / carrier protein

From a region of high concentration to a region of low concentration

Active transport and diffusion

. Active transport is against concentration gradient .

Diffusion down a concentration gradient.

2. Active transport requires ATP .

No ATP needed in diffusion.

3. Membrane proteins are involved in active transport which is not in diffusion.

Compare the processes of facilitated diffusion and active transport.

1. Both use membrane proteins

2. Facilitated diffusion goes down aconcentration gradient while active transport can transport against the
concentration gradient

3. Active transport uses ATP while

facilitated diffusion does not

Bulk transport

Transport of substances across the membrane by forming vesicles.

Endocytosis : transport of substances in to the cell by forming vesicles.

Exocytosis: transport of substances out of the cell by forming vesicles

Exocytosis: Pockets formed by the golgi apparatus fuse with the cell membrane to release macromolecules.
Many secretory cells use exocytosis to export products: nerve cells, pancreas… In endocytosis the cell takes in
macromolecules by forming new vesicles from the plasma membrane.

Vesicle
from golgi
apparatus

SUMMARY

Some molecules move across a cell surface membrane by passing down a concentration gradient, through the
phospholipid bilayer. The movement of some polar molecules across the membrane involves carrier and
channel PROTEIN molecules. When this movement occurs down a concentration gradient, the process is called
FACILITATED DIFFUSION And when it occurs against a concentration gradient the process is called ACTIVE TRANSPORT.

Energy in the form of ATP is used in the movement of molecules against a concentration gradient.

For each example below, suggest the type of transport most likely to be involved

Movement of oxygen across the wall of an alveolus……….DIFFUSION

Absorption of phosphate ions into root hair cells………… ACTIVE TRANSPORT

Pumping of calcium ions into storage vesicles inside muscle cells…… ACTIVE TRANSPORT
Release of glucose from liver cells into the blood stream……….. FACILITATED DIFFUSION

Removal of sodium ions that diffuse into a nerve cell, thus maintaining a low concentration within the nerve
axon…………… ACTIVE TRANSPORT

Reabsorption of water molecules from the kidney tubule………OSMOSIS

PRACTICE QUESTION

The transport of glucose across the cell membranes of liver

cells does not require energy.

Using information in the diagram, suggest how glucose is

taken into liver cells from the blood.

Answer

By facilitated diffusion down a concentration gradient

 ENZYMES

SPECIFICATION
(i) Understand the mechanism of action and the specificity of enzymes in terms of their three-
dimensional structure
(ii) Understand that enzymes are biological catalysts that reduce activation energy
(iii) Know that there are intracellular enzymes catalysing reactions inside cells and extracellular
enzymes catalysing reactions outside cells
What are enzymes?
Enzymes are biological catalysts and are proteins.
Every metabolic reaction within the living organism is catalyzed by an enzyme.
Biological catalysts
Enzymes that are produced by organisms that speeds up rate of metabolic reactions
Describe the structure of an enzyme.
Enzyme is a protein and have a 3D globular structure.
Bonds like ionic bond and disulphide bridge between the R groups help to hold the structure in place
It has specific active site in which only specific substrate molecule can bind.
Properties of enzymes
They are globular proteins.
They have specific active site where specific substrate molecules can bind.
Enzymes catalyze a reaction.
Reduce the activation energy needed for a chemical reaction to occur.
Do not alter the end product.
Remains unchanged at the end of a reaction
Two main groups of enzymes
Intracellular – occur inside a cell where they control metabolism E.g. Dehydrogenase in mitochondria
Extracellular- produced by the cell but their effect is outside the cell E.g- digestive enzymes
Enzyme specificity
Enzymes have very specific shape because of their tertiary and quaternary structure.
They can catalyze only specific reactions.
Active site of the enzyme is having specific shape.
Active site is the space where substrate molecule bind and specific substrate will fit the active site.
The specific active site gives enzyme its specificity.
Enzymes and Activation energy
Activation energy- energy needed for a reaction to occur by causing bonds to break / weaken / form
by increasing the number of collisions

1
Lowering activation energy
Enzymes combine with substrate molecule and form enzyme substrate complex which is temporary.
The attraction of oppositely charged group may distort the shape of the substrate(s) and assist in the
breaking of bonds or in formation of new bonds.
This reduces activation energy and increases the rate of reaction.

Theories explaining the formation of enzyme substrate complex

Induced fit theory:

Active site of the enzyme is flexible.

When the substrate enters the active site shape of the active site
modified to form the active complex.
Only specific substrate can change the shape of the active site.
Once the products have left the complex the enzyme returns to its
relaxed form.

Lock and key theory

Enzyme and substrate molecules fit together

like lock and key.
Active site is specific in shape and only those
substrates which have complementary structure
will combine with that enzyme.

2
Measuring initial rate of reaction
Initial rate of reaction is the rate at which the products are formed in an enzyme-controlled reaction
at the beginning.

3
Explain why the initial rate of reaction was measured in an enzyme-controlled investigation
At the start substrate is not a limiting factor.
As a reaction proceeds the concentration of substrate decreases.
Lower concentration of substrate limits rate of reaction.
Practice question
A student carried out an investigation into the rate at which grape juice produced quinone. The
graph shows the results of this investigation. Calculate the initial rate of this reaction.

Accept a straight line that must

through or between 19.0 mg cm-3 or
24.0 mg cm-3 at 30 s.
TE for mark points 2 and 3 from wrong
tangent
TE for mark point 3 for correct gradient
calculation with no tangent (y ÷ x)
Example of calculation:
21.0 / 30 = 0.70 mg cm-3 s-1
(accept range of between 0.63 mg cm3 s-1 to
0.80 mg cm3 s-1)

Casein is a protein that can be hydrolysed by the enzyme pepsin.

The graph below shows the effect of pepsin concentration on the hydrolysis of casein.

Calculate the initial rate of

hydrolysis for 8 units per cm3 of
pepsin.
Show your working.
- 0.5 ;
mg per 100 cm3 per minute / eq ;

Factors affecting the rate of enzyme action

Temperature and rate of enzyme action

As temperature increases up to optimum KE of the

molecules increases.
More effective collisions.
More enzyme substrate complexes formed.
Above optimum temperature more vibrations within
the molecule.
This break bonds like hydrogen and disulfide bonds.
Changes the shape of active site of the enzyme.
Substrate molecule can no longer fit to the active
site.

4
The effect of temperature on the rate of any reaction can be expressed
as the temperature coefficient, Q10.
This is expressed as :

Between 0⁰ C and 40 ⁰ C, Q10 for any reaction is 2- the rate of the reaction doubles for every 10 ⁰ C
rise in temperature.
Substrate concentration and enzyme action

As the substrate concentration increases the rate of reaction also increases as greater chance of
forming enzyme substrate complexes.

At optimum concentration of substrate molecules, all the active sites are occupied.
Further increase in substrate molecules will have no effect on the rate of reaction because no extra
active sites are to be used.
Enzyme is saturated.

Enzyme concentration on the rate of reaction

At low enzyme concentration, enzyme is the limiting

factor.
Increase in concentration of the enzyme increases the
rate of reaction as more active sites are available for the
substrate to bind.
At higher enzyme concentration, adding more enzyme
has no effect on the rate of reaction as substrate
molecule will be a limiting factor.

Explain the effect of enzyme concentration on the initial rate of the reaction.
At low enzyme concentrations enzyme is limiting / all active sites are occupied.
Increasing the enzyme concentration increases the number of active sites.
So more effective collisions and more ESCs formed per unit time.
Substrate is limiting at higher enzyme concentrations and not all of the {enzymes/active sites} are
occupied
5
The reaction rate (V) at each substrate concentration can be calculated using the formula

V max = the maximum rate of reaction

K is the substrate concentration when the rate of reaction is half the rate of V max
S is the substrate concentration
Practice question
The graph shows the relationship between substrate concentration and the rate of reaction of lactose

Calculate the reaction rate (V) at a substrate

concentration of 4a.u

correct values for Vmax and K read from the

graph
• correct answer for values substituted into
the formula

pH and enzyme action

Changes in pH affect the shape of the active site by changing ionic bonds within the enzyme.
This changes the rate of reaction.

A specific range of pH is needed for each enzyme to be active.

An enzyme is most active at its optimum pH.
Changes in pH affect the formation of hydrogen bonds and
disulfide bonds that hold the three-dimensional structure of the
protein together.
Changes in pH also affect the shape of the active site by
changing ionic bonds within the enzyme
This changes the rate of reaction.
To avoid this, use a buffer solution to make pH constant
Enzyme inhibitors
Active site directed inhibitors

Inhibitors bind to the active site preventing the substrate to bind

6
Non active site directed inhibitors

Inhibitors bind to the allosteric site, changing the shape of

the active site.
This prevent substrate from binding

Catabolic and anabolic reactions

Catabolic reactions
Reactions that breaks down large molecules
into simpler ones.
These are exergonic reactions
They have small activation energy.
The reaction products contain less energy
than the substrates.
Anabolic reactions

These are one that creating large

molecules out of smaller ones.
They are endergonic
Their activation energy is greater than
the reactants.
Extra energy must be supplied.

7
Explain the importance of the primary structure of an enzyme to its function.
Primary structure determines the three-dimensional folding
The type of amino acids determines types of bonds like hydrogen bond, ionic bond, disulphide bridge
Position of amino acids determines position of bonds
Shape and position of active site is determined by position of amino acids
Shape of active site should be specific to bind to substrate
How the primary structure of an enzyme determines its three-dimensional tertiary structure and its
properties.
Primary structure is the sequence of the amino acids in a polypeptide chain
This determines the position and the type of the bonds and folding
Determines the shape of the active site.
Polar or hydrophilic part on the outside of enzymes non polar or hydrophobic on the inside.
Different enzymes are involved in the formation of different carbohydrates using galactose and
glucose
Enzymes are specific due to the shape of active site
This allow only certain substrates to bind to form a complex.
Glucose molecule and Galactose molecule have different shapes

8
 Understand the nature of the genetic code (triplet code, non-overlapping and degenerate)

Know that a gene is a sequence of bases on a DNA molecule that codes for a sequence of
amino acids in a polypeptide chain.

understand the process of protein synthesis (transcription and translation), including the
role of RNA polymerase, translation, messenger RNA, transfer RNA, ribosomes and the role
of start and stop codons

(ii) Understand the roles of the DNA template (antisense) strand in transcription, codons on
messenger RNA and anticodons on transfer RNA.

understand how errors in DNA replication can give rise to mutations (substitution, insertion
and deletion of bases)

(ii) know that some mutations will give rise to cancer or genetic disorders, but that many
mutations will have no observable effect

Genetic code is the nucleotide base sequence on DNA (and subsequently on mRNA by
transcription) which will be translated into a sequence of amino acids of the protein to be
synthesized.
Codon is sequence of 3 bases on mRNA (e.g. ACG or UAG). Each codon is translated into one
amino acid.
Features of genetic code
Genetic code-The relationship between the sequence of bases on DNA and the sequence of
amino acid in a polypeptide chain.
The bases are read in a group of three bases- triplet code.
Codon- triplet code on mRNA coding for an amino acid
Genetic code is a triplet code- genetic code is a group of three bases which represent an
amino acid.

Explain why a triplet code is required for the synthesis of protein.

There are only four bases present but need to code for 20 amino acids. If it is a sequence of
two bases it can code for only 16 amino acids. So three bases is the minimum number that
provides sufficient combinations to code for each amino acid. Sequence of three bases gives
64 possibilities.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 1
Practice question
The maximum number of amino acids coded for by a molecule of mRNA that is 600 mononucleotides
long is …………….

Genetic code is degenerate- single amino acid can be represented by more than one genetic code.

GCU,GCC,GCA,GCG- Alanine

• Genetic code is non overlapping- each set of three bases forms one triplet. No base from one
triplet is part of another triplet. A sequence of nine nitrogen bases can code for three amino
acids.

Protein synthesis

Protein synthesis occurs in two steps- transcription and translation

Transcription is the process by which the DNA sequence is used to make a strand of mRNA in
the nucleus. Translation is the process by which the DNA code is converted into a protein in
the ribosome from the mRNA strand made in the nucleus.
Key players in protein synthesis
• mRNA carries the information from a gene in DNA.
• Ribosomes, made of rRNA, consist of subunits and
carry out an enzyme-like role.
• tRNA carries specific amino acids to the ribosome.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 2
Template strand for the synthesis of mRNA

The nucleotide sequence that directs the synthesis of complementary sequence /mRNA .

This is the part of the DNA / antisense strand that the mRNA is built along.

Gene : a sequence of bases on DNA on a chromosome which codes for a protein.

How a molecule of mRNA is made during transcription

• DNA unwinds by breaking hydrogen bonds between nitrogen bases

• RNA mononucleotides attach to antisense strand
• Complementary base pairing occurs between DNA and ribomononucleotides
• Mononucleotides are joined together by the formation of phosphodiester bonds by
condensation reaction by the enzyme RNA polymerase.
• mRNA detaches from the DNA
• DNA rewinds.

All the inrons are removed and exons are

joined together (spliceosome)

A poly adenine tail (3’) and a guanine cap

(5’) is attached to the ends of mRNA.

Form a mature mRNA.

Mature mRNA leaves the nucleus

through nuclear pore to cytoplasm.

Protein synthesis that occurs in the cytoplasm (Translation)

Ribosome attaches to mRNA start codon.

tRNA with specific amino acid (methionine)diffuse in to the ribosome.

Complementary base pairing occurs between anticodon on tRNA and codon on mRNA

Hydrogen bonds formed between the tRNA and mRNA

Bond between first tRNA and amino acid break and a peptide bond is formed between adjacent
amino acids by the enzyme peptidyl transferase by condensation reaction.

Then tRNA is released from the ribosome.

Ribosome attaches to next codon on mRNA.

The process continues until a stop codon is reached.

Unit 1/topic 2/biology/genetic code and protein synthesis
Page 3
Start codon

Smaller subunit of ribosome attaches to the start codon AUG and initiate translation.

Stop codon UAG UAA UGA

When the ribosome reaches a stop codon, there is no tRNA that binds to it.

Instead, proteins called “release factors” bind, and cause the ribosome, the mRNA, and the new
polypeptide to separate. The new polypeptide is completed. It stop the process of polypeptide
synthesis.

The importance of the sequence of bases in a gene.

Triplet coding system on DNA determines the codon on mRNA

Sequence of bases on mRNA determines order of amino acids

Primary structure is important in determining the 3D structure of protein ;

There is start sequences where ribosome attach for translation

Stop codons where translation stops.

Structure of tRNA

Transfer RNA molecules are short RNAs that fold into a characteristic

Clover leaf pattern.Each tRNA has 3 bases that make up the anticodon.

These bases pair with the 3 bases of the codon on mRNA during translation.

Each tRNA has an amino acid binding site (3’ end) where corresponding amino acid will attach.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 4
Anticodon: A sequence of three bases on tRNA that are complementary to the bases in the mRNA
codon.

Role of tRNA

Specific amino acid attaches to the amino acid binding site and form amino acyl tRNA complex
(amino acyl tRNA synthetase).

Transfer this into the ribosome from the cytoplasm.

Complementary base pairing occurs between codon on mRNA and anticodon on tRNA.

Ribosome structure and function

It consists of two sub units- a large sub unit and a small sub unit.

It is composed of proteins and rRNA.

It has three tRNA binding sites.

It help to hold the mRNA and two tRNAs in position during translation.

This help to assemble the growing polypeptide chain efficiently.

Polysome- a group of ribosome attached to a single mRNA during translation and leads to the
formation of large quantities of the same protein.

ROLE OF mRNA

mRNA is a copy of the DNA for the protein being synthesized

It moves out of the nucleus in to ribosomes in the cytoplasm. Also it acts as a template for translation

Sense strand: The DNA strand that carries the code for the protein to be formed.

Antisense strand (template strand): The DNA strand which acts as a template for an mRNA
molecule.

RNA polymerase: RNA polymerase attaches to the promoter region of the DNA.

This enzyme polymerises nucleotide units to form RNA in a sequence determined by the antisense
strand of DNA.

The roles of RNA molecules in protein synthesis

mRNA is produced by transcription and it leaves the nucleus through nuclear pore.

mRNA carries the genetic code for a protein . Also mRNA associates with ribosomes.

tRNA carries specific amino acid from cytoplasm to the ribosome for translation. tRNA and rRNA
holds amino acids in place for the formation of peptide bond between adjacent amino acids.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 5
Structure of tRNA molecule differs from the structure of a mRNA molecule

tRNA is folded and mRNA is straight

tRNA has hydrogen bonds but the mRNA does not

tRNA is a fixed size but mRNA length depends on size of gene

tRNA has an anticodon but mRNA has codons

tRNA has an amino acid binding site but mRNA does not.

Similarities in tRNA and mRNA

Both contain RNA (mono)nucleotides / ribose sugar / uracil (and adenine, cytosine and guanine) /
phosphodiester bonds and both are single stranded.
Differences between the processes of replication and transcription of DNA.

Mutation

Unpredictable change in the amount or the chemical structure of DNA.

Mutations are the ultimate source of all genetic variation.

Gene mutation

A change in the base sequence of DNA which can result in a new protein being produced.

The change in the base sequence is either due to addition or deletion or substitution of bases.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 6
Chromosome mutation

Changes in Chromosome Number or Structure.

A mutation that affects multiple genes. It occurs during mitosis and meiosis.

How a mutation could cause the structure to be altered

Changes in the sequence of bases in DNA / gene either by substitution/ deletion /addition

Changes the codon on mRNA (during transcription)

This could result in a different amino acid being carried by -

tRNA during translation.

This changes the primary structure of protein.

Resulting in different bonding (H-bond/disulphide bond)

Changing the shape of the 3D structure of protein and changes the shape of active site in enzymes.

So substrate molecule cannot bind.

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 7
Practice questions

(1) Galactose is broken down by an enzyme called Gal-1-PUT. In some types of galactosaemia, this
enzyme does not function properly.
Explain why a mutation in the gene coding for the enzyme Gal-1-PUT could lead to the inability to
break down galactose. (4)
1. change in DNA sequence / eq ;
2. idea of different mRNA ;
3. change in{amino acid /AA sequence/primary structure of protein}/reference to different R groups ;
4. idea of different { bonding / tertiary structure / 3D shape / folding } ;
5. change in {shape / properties} of the active site / enzyme not made ;
6. galactose does not fit in the enzymes active site /no enzyme available to break down galactose /eq

(2) Cystic fibrosis and glycogen storage disease type (II) are examples of recessive
genetic disorders. Glycogen storage disease type (II) is caused by mutations in the GAA gene. This
results in a deficiency of an enzyme called acid alpha-glucosidase.
Explain how a mutation in the GAA gene could result in a change in the activity of the enzyme acid
alpha-glucosidase. (5)

1. change in {DNA triplet / codons} ;

2. results in different {amino acids / amino acid sequence / primary structure} / eq ;
3. different R groups / different position of R groups ;
4. idea that this may change the bonding / named example of bonding ;
5. change in folding ;
6. therefore changing the {shape / structure} of the active site ;
7. idea that enzyme is unable to combine with its substrate

Unit 1/topic 2/biology/genetic code and protein synthesis

Page 8
 NUCLEIC ACID
Specification
(i) know the basic structure of mononucleotides (deoxyribose or ribose linked to a phosphate and a
base, including thymine, uracil, adenine, cytosine or guanine) and the structures of DNA and RNA
(polynucleotides composed of mononucleotides linked by condensation reactions to form
phosphodiester bonds)

(ii) know how complementary base pairing and the hydrogen bonding between two complementary
strands are involved in the formation of the DNA double helix

(i) understand the process of DNA replication, including the role of DNA polymerase

(ii) understand how Meselson and Stahl’s classic experiment provided new data that supported the
accepted theory of replication of DNA and refuted competing theories

Nucleic Acids DNA

• Examples:
– RNA (ribonucleic acid)
• single helix
– DNA (deoxyribonucleic acid)
• double helix
• Structure:
RNA
– monomers = nucleotides

Nucleotide
3 parts
nitrogen base (C-N ring)
pentose sugar (5C)
ribose in RNA
deoxyribose in DNA
phosphate (PO4) group
 Mononucleotide
of

RNA

Nitrogen bases
The nitrogen bases in DNA and RNA are
• pyrimidines C, T, and U.
• purines A and G.
Adenine (A), thymine (T), cytosine (C) and guanine (G) are the nitrogen bases present in DNA and
instead of Thymine nitrogen base Uracil is present in RNA.

Composition of DNA and RNA

Formation of mononucleotide
A mononucleotide contains three molecules linked together by condensation reactions removing two
water molecules:
A phosphate group and an organic base containing nitrogen attached to deoxyribose (a 5-carbon
sugar) by condensation reaction.
Dinucleotide formation
The sugar of one nucleotide joins to the phosphate radical of another nucleotide at position 3 by
condensation reaction and a water molecule is released.
Phosphodiester bond is formed between mono nucleotides.

Polynucleotide

The structure of DNA

 • DNA is a polymer of deoxyribonucleotides.
• Nucleotides are joined with phosphodiester bonds.
• Phosphodiester bonds are formed between the carbon-3 of the pentose of one and the
phosphate group of the next.
• Back bone of the DNA is made up of sugar and phosphate.
• Nitrogen bases are projecting outwards.
• DNA is made up of two polynucleotide chains and it is double stranded.
• Each chain has 5’ end and 3’ end.
• The two chains coil around each other and form a double helix.
• The double helical structure is held together by hydrogen bonds between the complementary
nitrogen bases.
• Pairing of nitrogen bases occurs between purines and pyrimidine.
• Complementary base pairing occurs between A and T and C and G.
• The two chains of the DNA are anti-parallel to each other.
• One chain runs from 5’ to 3’ and the other chain from 3’ to 5’.
• The base pairs are 0.34nm apart.
• There are 10 base pairs in one complete turn of the helix.
How mononucleotides combine to form a DNA molecule.
Phosphodiester bond formed between deoxyribose of one nucleotide and phosphate of another by
DNA polymerase
Complementary base pairing occurs and Hydrogen bonds form between bases
Methods of DNA replication
• Semi-conservative replication
• Conservative replication
• Dispersive replication

• Process of DNA replication

Replication is semi-conservative replication;

DNA molecule unwinds by breaking hydrogen bonds between nitrogen bases by helicase enzyme.
Mono nucleotides line up along both strands according to complementary base pairing. Hydrogen
bonds formed between bases.
Mononucleotides are joined together by phosphodiester bond by condensation reaction.
This is catalysed by the enzyme DNA polymerase.
(On completion of the process (copying the DNA) two identical daughter DNAs are formed.
Each newly formed double helix contains one of the polynucleotide chains of the parent DNA.
Meselsohn Stahl’s Experiment
Explain how Meselson and Stahl’s experiment provides evidence for the accepted theory for
the replication of DNA.
Meselson and Stahl’s experiment was designed to distinguish between different types of
replication;
At the start of the experiment cells were grown in (medium with) heavy nitrogen / 15N
Only a heavy DNA band was observed;
The cells were then transferred to (medium with) {light nitrogen / 14N } ;
After one generation an intermediate DNA band was observed;
After two generations intermediate and light bands were observed;
Showing that replication was {semiconservative / one strand of original DNA and one strand of
newly synthesised DNA;

The sequence of bases on part of one strand of a DNA molecule is:

ATCCCTGAGGTCAGT
What would be the sequence of bases on the corresponding part of the other strand?
Structure of RNA
It is a single polynucleotide strand.
It may be folded into complex shapes or remain as a long thread like molecules.
Compared to DNA they are very short in length.
Always single stranded.
The pentose sugar present in RNA is ribose.
Structure of a mononucleotide found in RNA.
1. contains {Ribose / 5C sugar / pentose} AND phosphate ;
2. reference to (nitrogenous) base / adenine / guanine / cytosine /
uracil / eq ;
Differences between the structure of DNA and the structure of RNA.
DNA is double stranded and RNA is single stranded
DNA has thymine while RNA has uracil
DNA has deoxyribose while RNA has ribose
DNA is larger than RNA
DNA and mRNA
DNA contain thymine but mRNA contain uracil
DNA has deoxyribose and (m)RNA has ribose
DNA is double stranded and (m)RNA is single stranded
DNA is helical and (m)RNA is straight
 GENETICS

SPECIFICATIONS

2.15:(i) understand what is meant by the terms gene, allele, genotype, phenotype, recessive, dominant,
codominance, homozygote and heterozygote
(ii) understand patterns of inheritance, including the interpretation of genetic pedigree diagrams, in the
context of monohybrid inheritance
(iii) Understand sex linkage on the X chromosome, including red-green colour blindness in humans

2.16: understand how the expression of a gene mutation in people with cystic fibrosis impairs the
functioning of the gaseous exchange, digestive and reproductive systems

2.17 :(i) understand the uses of genetic screening, including the identification of carriers,
Pre-implantation genetic diagnosis (PGD) and prenatal testing, including amniocentesis and chorionic
villus sampling
(ii) Understand the implications of prenatal genetic screening

2.18: be able to identify and discuss the ethical and social issues relating to genetic screening from a
range of ethical viewpoints, including religious, moral and social implications

Genetics- it is the science of inheritance.

Genes :sequence of nucleotides / bases in DNA coding for a polypeptide / protein.
Genome: it is the total set of genes in a cell
The nature of gene
It helps to determine an organism’s characteristics.
Genes must be able to reproduce themselves or replicate without losing the information.

Unit 1/ topic 2/ biology/ genetics Page 1

Allele: alternative form of a gene. This is responsible for a given contrasting character.
Genotype: the genetic constitution of an organism with respect to the alleles under consideration.
Phenotype: the physical characteristic of an organism
Resulting from the interaction between the genotype and the environment.
Recessive: allele which is expressed in the phenotype only in the absence of dominant allele
Dominant: allele which is expressed in the phenotype even if it is paired with alternative allele.
Homozygote: In homologous chromosomes, the diploid condition in which the alleles at a given locus are
identical. (TT,tt)

Unit 1/ topic 2/ biology/ genetics Page 2

Heterozygote: the diploid condition in which the alleles at a given locus are different. (Tt)

Locus – location of a gene on the chromosome

Homologous chromosome: chromosomes that contain DNA which carries the same gene

Codominance : In heterozygotes, where both alleles at a gene locus are fully expressed in the phenotype.
Example :
IA and IB are codominant. Here both the alleles are expressed and produce their proteins, which act
together without mixing. So the individual with both IA and IB will have both antigen A and B on the
surface of their erythrocytes and they will have the blood group AB.

Unit 1/ topic 2/ biology/ genetics Page 3

Monohybrid cross: A genetic cross where only one gene for one characteristic is considered
Sex linked traits: Characteristics which are inherited on the sex chromosomes.
Genes that are carried on the X chromosome are said to be sex-linked.
Recessive or mutant alleles on the X chromosome passed from a female parent to her male offspring will
be expressed in the phenotype because there is no corresponding allele on the homologous Y
chromosome.
Sex linked diseases in humans
A mother always donates an X chromosome to her sons. The father always donates the Y chromosome.
Any mutations in a gene on the X chromosome will affect the phenotype of the offspring, even if the
characteristic it codes for is recessive. This is because the Y chromosome is small and carries only genes
which code for traits associated with maleness.
Red green colour blindness in human

The ability to see in colour is the result of multiple genes coding for different aspects of the process.
Many of these genes are found on the X chromosome. Mutations in these genes can affect our ability to
see in colour, causing different types of colour blindness. Red green colour blindness is the result of one
of these mutations.
Red green colour blindness is caused by a recessive mutation of a gene on the X chromosome. It is much
more common in men than in women because the condition is sex linked.
How gene mutation can affect the phenotype
Mutations can produce variation within an organism.
If the different arrangements of nucleotides code for the same amino acid, a point
mutation will have no effect.

Unit 1/ topic 2/ biology/ genetics Page 4

If by mutation a new and a superior protein is produced, the organism may gain a
reproductive advantage so that it leaves more offspring than other individuals of that
species, particularly when environmental condition changes.
Most mutations are neutral, which means that they neither improve nor worsen the
chance of survival.
Some mutations cause much damage, disrupting the biochemistry of the whole organism
by changing the shape of the active site of the enzyme.
Random mutations in the genetic material of the gametes are cause of many human
genetic diseases like thalassemia and cystic fibrosis.
Thalassemia- blood proteins are not manufactured correctly
Cystic fibrosis- membrane protein does not function properly
Mutations in the somatic cells of the body as they divide results in many different types of
cancer, depending on where in the body they occur.
However, most mutations will have no observable effects on the organism. This may be
because:
The mutation occurs in part of the non- coding DNA which does not affect the way the
genetic code is read.
The code is degenerate, and a small change in the code may not alter the amino acid
coded for.
Cystic fibrosis (CF)- Mucus become thick and sticky due to mutation in CFTR gene
It is due to the mutation in CFTR gene in the 7th chromosome.
CFTR- cystic fibrosis transmembrane conductance regulator gene.
This gene codes for a protein called CFTR protein.
This protein is essential for chloride transport which is located on the apical membrane
of mucus secreting cells.
Water content in the mucuc is regulated by the transport of sodium and chloride ions
across the epithelial cells.

Unit 1/ topic 2/ biology/ genetics Page 5

Hundreds of different mutations in the gene can give rise to CF.
These mutations affect the CFTR protein in different ways.
In some cases ATP is unable to bind and open the ion channel.
In some other cases channel is open but reduce the movement of chloride ions through
the channel.
Regulating water content in mucus in a person without CF

Unit 1/ topic 2/ biology/ genetics Page 6

A person with CF
Mutation in the CFTR gene
CFTR protein may be missing or if present it does not function properly.
Chloride ions are actively transported in to the epithelial cells from the tissue fluid.
There is a high concentration of chloride ions in the epithelial cells.
Creates a concentration gradient between the cell contents and the fluid on the surface of
the cell.
The faulty CFTR channel protein remains shut.
This prevents the chloride ions from diffusing out.
Sodium gated channels are always open.
So sodium ions diffuse in to the cell.
There is a high concentration of sodium and chloride ions in the epithelial cell.
Water moves from the mucus in to the epithelial cell by osmosis.
Mucus become thick and sticky.

Unit 1/ topic 2/ biology/ genetics Page 7

The effects of CFTR
CF affects different systems of the body
Respiratory system
Digestive system
Pancreas
Reproductive system
CF and Respiratory system
Thick mucus builds up in the tiny airways.
Bronchioles become blocked with mucus.
This reduces the SA for gas exchange.
The person feels tired and breathless.
Repeated infections and blockage cause severe lung damage.
CF and Reproductive system
CF leads to infertility in both males and females.
Males
Men with CF lack sperm duct or it may be partly blocked by thick mucus.
This prevents sperm movement in to the duct.
Leads to reduced sperm count and infertility.
Females
The entry of sperm is prevented by the thick mucus in the cervix.
Thick mucus also block the oviduct and implantation is impaired .
Thick mucus in the reproductive system affect the movement of egg
CF and Digestive system
CFTR channel not function properly
Produces thick and sticky mucus in the pancreas.
Mucus blocks pancreatic ducts
Digestive enzymes cannot be secreted into small intestine.

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This reduces digestion and absorption of food which leads to malnutrition and weight
loss.
Accumulation of pancreatic juice leads to self-digestion of pancreatic cells .
There will be problems controlling blood sugar levels .
It is necessary to test for several different recessive alleles in the screening for cystic
fibrosis.
Cystic fibrosis results from one of a number of possible mutations of this gene
Testing for only one will miss other recessive alleles.
Treatments of CF
Medication
Bronchiodilators :- relax the muscles in the airways. Relieving the tightness of the chest.
Antibiotics :- used either to kill or prevent the growth of bacteria in the lungs.
DNAase enzyme:-
Infection of the lungs leads to the accumulation of WBC in the mucus.
Break down of this WBC releases DNA which add to the stickiness of the mucus.
DNAase enzyme breakdown the DNA. The mucus is easier to clear from the lungs
Diet
Adults with CF are recommended to eat high energy food.
Diet should include double the quantity of protein.
Should also take salt supplements.
Digestive enzyme suppliments:
This help to complete the process of digestion.
Physiotherapy :
This causes changes in the air pressure within the airways.
This vibration aid movement of mucus.
This loosen the mucus and improve the flow of air into and out of the lungs.

Unit 1/ topic 2/ biology/ genetics Page 9

GENETIC SCREENING
Procedure used to examine an individual for the presence of a genetic
disease.

Uses

(1) to confirm a diagnosis

(2)to identify carriers

(3) prenatal screening

(4) pre implantation genetic diagnosis (PIGD)

PRENATAL SCREENING
A modern technique to identify any health problems of the unborn baby.
It is possible to provide counseling about the quality of life the child can expect in the
society.This include:
Amniocentesis
Chorionic villus sampling
AMNIOCENTESIS
20 cm3 of amniotic fluid removed from amniotic sac of mother at 16th week of pregnancy.
Isolate fetal / embryonic cells present in amniotic fluid and analyse the DNA to detect
defective gene(s)

Unit 1/ topic 2/ biology/ genetics Page 10

Disadvantage
Abortion affects both physically and mentally.
Results obtain only after 4 weeks.
It is a regrettable delay if abortion is to be carried out.
1% risk of spontaneous abortion after the procedure.
CHORIONIC VILLUS SAMPLING
Placental tissue is removed from the womb of mother.
Isolate the fetal cells present in placenta.
Analyse the DNA to detect defective gene.

Advantage
It can be carried out early in pregnancy.
If a decision is made to abort the fetus, the abortion is less difficult and risky.

Disadvantage
2.5-4.8% risk of spontaneous abortion after the procedure.
All paternal X chromosomes are inactivated in fetal placental cells.
So any problems in the genes on that chromosome cannot be detected by this technique.
PREIMPLANTATION GENETIC DIAGNOSIS: PIGD
Allow the gametes to fuse outside the body.
Collect the cell at early stage of IVF embryo.
Analyze the DNA of embryo
Detect the mutant allele.

Unit 1/ topic 2/ biology/ genetics Page 11

Advantage and disadvantage to the parents of genetic screening of their fetus.
Advantage
Prevent child dying late in pregnancy
Less stress for parents
Parents can prepare for child with / without the disorder.
Making an informed choice.
Disadvantage
Risk of miscarriage of healthy child.
More stress for parents.
Cost.
Risk of false negatives / positives
Genetic screening- issues
Embryo is having the right to live ; abortion is murder
A false positive result may leads to abortion of healthy fetus.
Who has right to decide if tests should be performed.
Future medical costs so parents can prepared.
Issues related to confidentiality of parents / child may arise .Eg paternal DNA does NOT
match.
If abnormality is found, parents may think about abortion.
Also there will be problems with future employment / insurance.
Risk of miscarriage so loss of fetus / risk to mother.
Give stress to parents this leads to increased risk of miscarriage.

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