Oxygen Transport in Blood

At the end of the lecture, students should be able to:

• Define common respiratory pigments (oxygen carriers).

• Give examples of animals that use these respiratory

pigments.

• Define, draw and briefly explain the significance of oxygen

dissociation curve.

• List some factors that affect Hb and O2 binding and how they
influence the shifting of the curve.
Circulatory System – Overview, blood flow through the body

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 Oxygen Transport in Blood

Oxygen Transport in Animals

Invertebrates
• Diffusion too slow except in smallest organisms
• Oxygen carried in blood (haemolymph) in simple physical
solution in many invertebrates.

Vertebrates (almost without exception)

• Dissolved O2 not enough.
• Oxygen carriers used to transport greater amount of O2
• Oxygen carriers (metal-containing proteins) often called
respiratory pigments.
 Oxygen Transport in Blood
Respiratory pigment
• A molecule that increases oxygen-carrying capacity of the blood.

Common respiratory pigments (oxygen carriers)

• Haemocyanin
- A complex copper-containing extracellular protein carried in solution.

- This metalloprotein contains two copper atoms that reversibly bind a

single oxygen molecule (O2).

- Second only to haemoglobin in frequency of use as an oxygen transport

molecule.

- Unlike Hb in vertebrate red blood cells, haemocyanins are not bound

to blood cells but are suspended directly in haemolymph.
 Oxygen Transport in Blood
Common respiratory pigments (oxygen carriers)
• Haemocyanin
- Oxygenation causes a color change between the colourless Cu(I)
deoxygenated form and the blue Cu(II) oxygenated form.
- Occurs in molluscs, arthropods (e.g. spiders and scorpions), crabs,
lobsters, among others.

• Haemerythrin
- Iron-containing intracellular protein.
- Occurs in cells in polychaetes, among others.
- Myohaemerythrin is O2-binding protein found in the muscles of marine
invertebrates.
- Haemerythrin and myohaemerythrin are essentially colorless when
deoxygenated, but turn a violet-pink in oxygenated state.
 Oxygen Transport in Blood
Common respiratory pigments (oxygen carriers)

• Chlorocruorin
- Iron-porphyrin protein

- Carried in solution in some polychaetes

- Oxygenated chlorocruorin turns from green to red.

 Oxygen Transport in Blood
Haemoglobin
• Iron-containing oxygen-transport metalloprotein in the red
blood cells of all vertebrates (Anthea et al., 1993) except
fish family Channichthyidae (Bruce and O'Brien, 2006) and
tissues of some invertebrates.

• Is a tetramer consisting of 4 polypeptide protein chains,

(globins), which are usually:
- 2 alpha chains (each 141 amino acids long)
- 2 beta chains that are each 146 amino acids long
• Attached to each chain is an iron-containing molecule known
as haem.

A haem molecule
 Oxygen Transport in Blood
Haemoglobin
• Iron-porphyrin protein that is carried in solution or in cells

• bright red when oxygenated and dark red (purplish) when

deoxygenated.

• Occurs in almost all vertebrates, some molluscs, arthropods,

annelids, nematodes, trematodes, protozoa, among others.

Oxygen physically dissolved in mammalian blood is

0.2 ml O2 per 100 ml blood
Amount of O2 bound reversibly to haemoglobin is about
20 ml O2 per 100 ml blood (Schmidt-Nielsen, 1990).
 Oxygen Transport in Blood
Oxygen carriers

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 Oxygen Transport in Blood
Oxygen binds reversibly to haemoglobin molecule.
HHb + 4O2 HbO8 + H+

Oxygen dissociation curve

• Oxyhaemoglobin dissociation curve relates oxygen saturation (sO2) and
partial pressure of oxygen in blood (pO2). Determined by Hb affinity for
oxygen.
• Oxygen–haemoglobin dissociation curve plots the proportion of Hb in its
saturated form on the vertical axis against prevailing oxygen tension on
the horizontal axis.

• It is an important tool for understanding how our blood carries and

releases oxygen.
 Oxygen Transport in Blood
Oxygen dissociation curve
• Draw curve

• Hb combines with oxygen to form oxyhaemoglobin (HbO2) at high oxygen

concentration.

• At low oxygen concentration, O2 is given up & the reaction proceeds to the

left. Hb gives up all O2 it carries when O2 concentration is reduced to zero.

• Each iron atom in Hb molecule binds one oxygen molecule.

• When all available binding sites are occupied, Hb is fully saturated and
cannot take any more O2 even at high concentration.
 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
• Temperature
- Increased temperature weakens bond between Hb and O2
-- What is its physiological importance in cold- and warm-blooded
animals?
- Increased metabolic rate (need for oxygen) in cold-blooded animals
- In fever or in exercise, oxygen consumption rises in warm-blooded
animals. Where will the curve shift to?
• pH
- Decrease in pH (increase in H+ ion concentration) shifts curve to the
right. Reason: H+ & O2 both compete for binding to the haemoglobin
molecule.
- Hb binds less O2 for a given PO2 with increased acidity (Bohr effect,
Jacquez, 1979).
 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
• Carbon dioxide

- Increased CO2 or other acids lowers plasma and intracellular pH (the

Bohr effect).

- CO2 binds to terminal amino groups of Hb forming

carbaminohaemoglobin.

- Only about 5–10% of CO2 content of blood is transported as carbamino

compounds. Most of the CO2 content (80–90%) is transported as
bicarbonate ions (HCO3-).
- Elevated CO2 content creates respiratory acidosis (medical condition in
which decrease in ventilation causes increase in blood CO2 conc. &
decreased pH (acidosis).
-- What is the effect on the curve?
 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
• Organic phosphate compounds
- Examples: 2,3-Diphosphoglycerate (2,3-DPG), ATP, inositol
pentaphosphate (IPP), guanosine triphosphate (GTP).

- IPP (dominant in birds, but no DPG), ATP and GTP (high in fish).

- Humans, horse, dog, rabbit, guinea pig and rat have high DPG sensitive
to their Hb. But sheep, goat, cow and cat have low DPG with low
interaction with Hb (Bunn, 1971)

- 2,3-DPG is created in erythrocytes during glycolysis. Its production

increases in the presence of diminished peripheral tissue O2 availability.

- Hb combines with 2,3-DPG and lowers affinity of Hb for O2.

 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
Altitude
• Lower atmospheric pressure at high altitude means lower oxygen partial
pressure than at sea level.

• Animals living at higher altitudes have adaptations

for oxygen uptake.

- E.g. Llama lives in high Andes of South America

(often above 5000 m) and its Hb has high O2
affinity.
- Llama brought up in a zoo at sea level has
similar affinity.

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 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
Altitude
• At high altitude humans gradually become adapted to low O2 pressure,
performs better physically & mentally.

- Curve shifts to the right (increased DPG levels) to augment O2 delivery

to tissues.
• Thus a given curve can be regarded as a trade-off between desirable O2
affinity and equally desirable low affinity.
 Oxygen Transport in Blood
Factors affecting Hb & O2 binding
• Carbon monoxide (CO)
- Hb binds with carbon monoxide 200–250 times
more readily than with oxygen (Jacquez, 1979).

- CO is highly successful competitor. Even at

minuscule partial pressures, CO can displace
O2 and results in a shift of the curve to the left.

- Hb is more than 50% saturated with CO at a CO

partial pressure of less than 1 mm Hg.

- One can suffer from severe tissue hypoxia while dr-amy.com

maintaining a normal pO2.

 Oxygen Transport in Blood
Foetal & maternal haemoglobins
• Foetal Hb (HbF) is structurally different from normal adult Hb (HbA).

- HbF structure: two gamma & two alpha chains.

- Adult Hb (HbA) is made of two alpha & two beta chains.

• Foetal arterial oxygen pressures are lower than adult arterial oxygen
pressures. Higher affinity to bind O2 is required to allow diffusion across
placenta.

• Higher concentration of 2,3-DPG is formed at the placenta.

• 2,3-DPG binds more readily to adult Hb (i.e. beta chains) and not to HbF
(i.e. gamma chains) hence HbF is not affected (Lippincott et al., 2007).

• Curve shifts to the left. HbF delivers O2 to tissues that have even lower
partial pressures.
What is the physiological significance?