Hormones, proteins, enzymes

HORMONES
Hypothalamus and
Posterior Pituitary

Midsagital view
illustrates that
magnocellular neurons
paraventricular and
supraoptic nuclei
secrete oxytocin and
vasopressin directly
into capillaries in the
posterior lobe
 Anterior pituitary:
adenohypophysis
 Anterior pituitary: connected to the
hypothalamus by the superior
hypophyseal artery.
 The anterior pituitary produces six
peptide hormones:
 prolactin,
 growth hormone (GH),
 thyroid stimulating hormone (TSH),
 adrenocorticotropic hormone (ACTH),
 follicle-stimulating hormone (FSH),
 and luteinizing hormone (LH).
ADRENAL GLANDS
Epinephrine/ Adrenaline
Levarterenol or
norepinephrine
Dopamine or 3,4-
dihydroxyphenyethylamine
THYROID GLAND
Thyroxine (T4)-
metabolism growth
Triiodothyronine (T3)-
Catabolism, body heat
production
Sodium liothyronine
Liotrix
Sodium dextrothyroine
 Hyperthyroidism
(thyrotoxicosis),T3
and T4
 Grave’s disorder/ Parry’s
disorder/ Basedow’s
disorder/ Exophthalmic
goiter/ Toxic Diffuse
goiter
 Tachycardia,
Hypertension, weight loss,
heat intolerance, pliable
nails
 Hyperthyroidism
(thyrotoxicosis),T3
and T4

 Restlessness, nervousness,
irritability, agitation
 Increased metabolic rate
(due to hypersecretion of T3)
 Increased body temperature
(due to hypersecretion of T4)
 Hypocalcemia (due to
hypersecretion of
thyrocalcitonin)
2/6/2018
Hypothyrodism
 Results from deficiency
of thyroid hormones
 Myxedema (adult)
 Cretinism (children)
Posterior Pituitary
(Neurohypophysis)
Oxytoxin
Vasopressin (ADH)
 Hypersecretion:
SIADH (symptom of
Inappropiate Anti- Diuretic
Hormone)
 Hyposecretion: Diabetes
insipidus
PANCREAS
Glucagon – alpha cells of
Islet of Langerhans
serum glucose levels
(glucogenolysis)
Insulin – Beta cells of Islet
of Langerhans
serum glucose levels
Proteins and enzymes
 Proteins
 are polymers of amino acid joined together
by peptide bonds.
 Loss of tertiary structure results in
denaturation of the protein and loss of
activity.
 What is the difference
between a Protein and a
Peptide?

ANSWER: The distinction between proteins and peptides

is one of length of the amino acid chain and molecular
weight and is somewhat arbitrary, but generally
polypeptide chains in excess of 50 to 75 amino acids
(molecular weight of 5000 daltons to 7500 daltons) are
considered proteins instead of peptides.

2/6/2018
PROTEIN RICH SOURCES
 Denaturation can be induced by any
condition that disrupts the stabilizing forces
such as salts, organic solvents, extremes of
pH, heating and freezing, and detergents,
although various proteins will have varied
sensitivities to different denaturants.
 Primary Structure of
Proteins
The particular sequence of amino acids that is
the backbone of a peptide chain or protein
CH3
CH3 S
CH CH3 SH CH2
CH3 O
+ CH O CH2 O CH2 O
-
H3N CH C N CH C N CH C N CH C O
H H H
Ala-Leu-Cys-Met
2/6/2018 22
 Secondary Structure – 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”

2/6/2018 23
Secondary Structure – Beta
Pleated Sheet
 Polypeptide chains are arranged
side by side
 Hydrogen bonds form between
chains
 R groups of extend above and
below the sheet
 Typical of fibrous proteins such
as silk

2/6/2018 24
 Secondary Structure –
Triple Helix
 Three polypeptide chains woven
together
 Glycine, proline, hydroxy proline
and hydroxylysine
 H bonding between –OH groups
gives a strong structure
 Typical of collagen, connective
tissue, skin, tendons, and
cartilage

2/6/2018 25
 Learning Check

Indicate the type of structure as:

(A) primary
(B) alpha helix
(C) beta pleated sheet
(D) triple helix
C. Beta pleated sheet

Polypeptide chain held side by side by H

bonds.
2/6/2018
 Learning Check

Indicate the type of structure as:

(A) primary
(B) alpha helix
(C) beta pleated sheet
(D) triple helix
A. Primary

Sequence of amino acids in a polypeptide

chain.
2/6/2018
 Learning Check

Indicate the type of structure as:

(A) primary
(B) alpha helix
(C) beta pleated sheet
(D) triple helix
B. Alpha helix

Corkscrew shape with H bonds between

amino acids.
2/6/2018
 Learning Check

Indicate the type of structure as:

(A) primary
(B) alpha helix
(C) beta pleated sheet
(D) triple helix
D. Triple helix

Three peptide chains woven like a rope.

2/6/2018
ENZYMES
 Organic catalysts
produced by living
organisms
 Common properties:
They are colloids and are
soluble in water and dilute
alcohol and are
precipitated by
concentrated alcohol
SUBSTRATE
 Most enzymes act best at temperatures
between 35 and 40 °C; temperatures above
65°C, especially in the presence of moisture
usually destroy them, whereas their activity is
negligible at 0°c
 Certain heavy metals, formaldehyde and free
iodine retard the enzyme’s activity
 Activity is highly
affected by the pH of
the medium in which
they act or by the
presence of other
substances in the
medium

2/6/2018
If the enzyme is combined with organic
substance, the non protein organic substance is
termed as COENZYMES.
If the enzyme is combined with inorganic ions,
the non protein organic substance is termed as
activators
6 major classes of enzymes
1. Oxidoreductases

 Catalyzing
oxidoreductions
between two
substances

2.Transferases

 Catalyzing a transfer of
a group, other than
hydrogen, between a
pair of substances
6 major classes of enzymes

3. Hydrolases

 Catalyzing hydrolysis
of ester, ether,
peptide, glycosyl,
acid anhydride, C-C,
C-halide, or P-N
bonds
6 major classes of enzymes

4. Lyases

 Catalyzing the
removal of groups
from substrates by
mechanisms other
than hydrolysis,
leaving double bonds

2/6/2018
6 major classes of enzymes
5. Isomerases

 Catalyzing
interconversion
of optic,
geometric, or
positional
isomers
6 major classes of enzymes
6. Ligases
 Catalyzing linkage of
two compounds
coupled to the
breaking of a
pyrophosphate bond
in ATP or a similar
compound.

2/6/2018
Amylolytic enzymes or
carbohydrases
 Two well known amylolytic enzyme
 Diastase and amylase- Two well known amylolytic
enzyme

 Salivary diastase or ptyalin and pancreatic diastase

or amylopsins are found in the digestive tract of
animals. They are sometimes called animal diastase

 Malt diastase is formed during the germination of

barley grains and converts starch into maltose. It is
most active in solutions that are approximately neutral;
acidity of pH 4 destroys the enzyme
 carbohydrases

Invertase or sucrase
Found in the yeast and in intestinal juices
carbohydrases
Maltase
Causes the conversion of maltose into glucose,
is also found in yeast and intestinal juices
carbohydrases
Zymase
Fermenting enzyme causing the conversion of
monosaccharides into alcohol and carbon
dioxide
carbohydrases
Emulsin
Enzyme found in almonds.
It causes the hydrolysis of Beta-glucosides
Amygdalin = benzaldehyde and HCN
carbohydrases
Myrosin
Found in white and black mustard
It hydrolyses sinalbin, sinigrin and other
glycosides
Esterases
Lipase
A lipolytic enzyme widely distributed in the plant and
animal kingdom
It is found in the pancreatic juice of animals oily seeds
It causes the hydrolysis of fats into glycerin and fatty acids
Esterases
Pectase
Spilts pectin into pectic acid and methyl
alcohol
Esterases
Steapsin
A lipolytic enzyme
capable of digesting
dietary fat
Ureases
Obtained from soybean
Used as a laboratory
agent for converting urea
to ammonia
Esterases

 STEATORRHEA
Proteolytic enzymes
Pepsin
A proteolytic enzyme found in the gastric juice
Most active at pH 1.8, but in neutral or alkaline
media, pepsin is entirely inactive.
It converts proteins into proteoses and
peptones
 Proteolytic enzymes
Trypsin
Formed when the proenzyme, trypsinogen, is acted on by the enterokinase of
the intestinal juices.
A proteolytic enzyme that is considerably more active than pepsin, converting
proteoses and peptones into polypeptides and amino acids.
It acts best in alkaline medium of about pH 8 and may thus be distinguished
from pepsin, which acts only in acid media.
Proteolytic enzymes
Erepsin
A proteolytic enzyme found in intestinal juices.
It converts proteoses and peptones into amino
acids.
Proteolytic enzymes
Renin
Is a coagulating enzyme
present in the mucous
membrane of the stomach of
mammals. It curdles the
soluble casein of milk

Papain
A mixture of active
proteolytic enzyme found in
the unripe fruit of papaya tree.
It is used as meat tenderizer
Oxidizing enzymes
Peroxidases
Are widely distributed in plants. They bring
about the oxidation reactions that cause the
discoloration of bruised fruits.
Oxidizing enzymes
Thrombin
Converts the fibrinogen
of the circulating blood
into the insoluble fibrin of
the blood clot
Zymase
Although splitting
monosaccharides, is
essentially an oxidizing
enzyme because the
monosaccharide is split
by oxidation
 Malt extract
Malt or Malted barley
 Is dried, artificially germinated barley grain
 It resembles barley but is more crisp, has an
agreeable odor and has a sweet taste.
 Used in brewing and alcohol industries
Malt extract
 Is the product obtained by extracting malt, the
partially and artificially germinated grain of one or
more varieties of Hordeum vulgare.
Use(s)
 Used as an easily digested nutrient
 As an aid in digesting starch
Malt extract
BARLEY
Dried grain of one or more varieties of
Hordeum vulgare Linn. Graminae
Diastase
 Is a yellowish white, amorphous powder
obtained from an infusion of malt. It can convert
50 times its weight of potato starch into sugars.
Lactase
 An enzyme that hydrolyzes LACTOSE into GALACTOSE
AND GLUCOSE
 It is obtained commercially from yeast
PEPSIN
 A substance containing a proteolytic enzyme obtained from the
glandular layer of the fresh stomach of the hog, Sus scrofa.
 Scaly pepsin-pepsin allowed to dry in glass plates
 Spongy pepsin-pepsin evaporated in vacuum
 Use
 Administered to assist gastric digestion
PANCREATIN
 Is a substance containing principally AMYLASE, LIPASE,
and PROTEASE
 It can be obtained from the pancreas of the hog or of the
ox
 Uses
 a digestive aid
 used in the preparation of predigested foods for the invalids
 Enteric coated granules have been used to treat infants with celiac
disease and related pancreatic deficiencies
Pancrelipase
 Is essentially a more concentrated from
of PANCREATIN
 Uses
 As a digestive aid
 Pancrelipase increases the intestinal absorption of fat,
thus aiding in the control of steatorrhea
CHYMOPAPAIN
 A non pyrogenic proteolytic enzyme obtained from the latex of Carica
papaya
 Use
 Employed in the treatment of herniated lumbar
intervertebral disk
BROMELAINS
 Bromelain or Bromelain is the mixture of protein digesting and milk
clotting enzymes obtained from the juice of pineapple plant, Ananas
comosus.
 Use(s)
 adjunctive therapy to reduce inflammation and edema
 Accelerate tissue repair especially following episiotomy
TRYPSIN
 Crystallized trypsin is a proteolytic enzyme crystallized
from the pancreas of the ox, Bos Taurus (Bovidae)
 Use
 Used for debridement of necrotic and pyogenic
surface lesions
CHYMOTRYPSIN
 is a proteolytic enzyme crystallized from the pancreas
of the ox, Bos Taurus (Bovidae)
 available as chymotrypsin for ophthalmic solution
HYALURONIDASE
 Hyalunoridase for injection is sterile, dry, soluble, enzyme product
prepared from mammalian testes and capable of hydrolyzing
mucopolysaccharides of the type of hyaluronic acid
 Use
 SPREADING AGENT
STREPTOKINASE
 Is a purified bacterial protein elaborated by group c beta hemolytic streptococci. It is
supplied as lyophilized powder. It acts to convert plasminogen to the proteolyic
enzyme plasmin. PLASMIN degrades no only fibrin clots but also fibrinogen and other
plasma proteins
 Use
 It is indicated for pulmonary embolism, deep vein thrombosis and embolism,
arteriovenous cannula occlusion and coronary artery thrombosis
UROKINASE
 Isolated from the human urine or obtained from human kidney cells by tissue culture
techniques
 It acts on the endogenous fibrinolytic system converting plasminogen to the enzyme
plasmin. PLASMIN degrades no only fibrin clots but also fibrinogen and other plasma
proteins
 Use
 It is indicated for pulmonary embolism, arteriovenous cannula occlusion and restoring
the patency of intravenous catheters
FIBRINOLYSIN
 It is in the blood serum as a protease and in plasma fraction with streptokinase
 Use
 It is used primarily in the treatment of blood clots within the cardiovascular system,
exclusive of the thrombi of the coronary and cerebral arteries
SUTILAINS
 Is a substance containing
proteolytic enzymes derived from
the bacterium Bacillus subtilis
 It is used for wound debridement

COLLAGENASE
 Is an enzyme preparation obtained
from the fermentative cultures of
Clostridium histolyticum
 It cleaves collagen and is used
topically to debride dermal; ulcers
and severely burned areas

L- ASPARIGINASE
 Is an enzyme obtained from the
cultures of E. coli
 Use
 Antitumor agent