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HaemoglobinΓÇÖs Role in Oxygen and Carbon Dioxide Transport

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0% found this document useful (0 votes)
19 views34 pages

HaemoglobinΓÇÖs Role in Oxygen and Carbon Dioxide Transport

Uploaded by

tsteadman
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Haemoglobin’s role in

oxygen and carbon dioxide


transport
The Role of Partial Pressure
Gradients
• Diffusion of a gas depends on
differences in a quantity called partial
pressure.
• A gas always diffuses from a region of
higher partial pressure to a region of
lower partial pressure.
The Role of Partial Pressure
Gradients

• In the lungs and in the tissues, O2


and CO2 diffuse from where their
partial pressures are higher to
where they are lower.
Respiratory Pigments
• Most vertebrates and many invertebrates have
evolved a group of coloured proteins
(respiratory pigments) capable of loosely
combining with oxygen, in order to increase
the oxygen-carrying capacity of blood.
• These pigments with large relative molecular
mass are found in the plasma while those of
smaller relative molecular mass occur within
cells to prevent them being lost by
ultrafiltration in the kidneys.
Property of respiratory pigments:

• They can combine readily with oxygen where


its concentration is high, i.e. at the lungs ,
• and to release it as readily where its
concentration is low, i.e. in the tissues.
• E.g. haemoglobin in mammals
Oxygen Transport
• Method Percentage
• Dissolved in Plasma 1.5 %
• Combined with Hemoglobin 98.5 %

Bound to Hgb
Dissolved
Haemoglobin Structure
Protein made up of 4 subunits
Every subunit contains a haem moiety attached to a
polypeptide chain.

9
Oxyhaemoglobin Formation
• An oxygen molecule reversibly attaches
to the haem portion of hemoglobin.
• The haem unit contains iron ( +2 ) which
provides the attractive force.

O2 + Hb HbO2
Haemoglobin:
• best known & most efficient respiratory
pigment in most animals
• an Fe porphyrin compound (haemo group)
• and a protein (globin);
• globin group varies in different species but
the haem group is always the same
• each human haemoglobin has 4 haem
groups and can carry 4 O2
•In normal adults, most of the
haemoglobin contains 2α and 2 β chains.

•Each of the 4 iron atoms can bind


reversibly on O2 molecule.

•The iron stays in the ferrous state, so


that the reaction is an oxygenation, not an
oxidation.
•When saturated with O2 (4 O2 in one
haemoglobin molecule), it is always
written Hb4O8.

•The reaction is rapid, requiring less than


0.01 second.

•The deoxygenation (reduction) of Hb4O8


is also very rapid.
Basic Concepts:
• Oxygen Capacity : The maximum quantity of
oxygen that will combine chemically with the
hemoglobin in a unit volume of blood;
normally it amounts to 1.34 ml of O 2 per gm of Hb or
20 ml of O2 per 100 ml of blood.

• Oxygen Content: how much oxygen is in the blood

• Oxygen Saturation : A measure of how much


oxygen the blood is carrying as a percentage of the
General properties of the oxygen
dissociation curves:
1. An efficient respiratory pigment readily
picks up oxygen at the respiratory surface
and releases it on arrival at tissues.

2. Respiratory pigments have a high affinity


for oxygen when its concentration (in
terms of partial pressures/tensions) is
high, but reduced when the oxygen
concentration is low.
The oxygen-hemoglobin dissociation curve:

the curve
relating
percentage
saturation of
the O2-carry
power of
hemoglobin to
the PO2.

16
The oxygen-hemoglobin dissociation curve

A. Flattened upper portion

B. Steep middle portion

C. Lower portion

17
Shifting the Curve

18
One factor that Shift the
Oxygen-Hemoglobin
Dissociation Curve:
• increased CO2 leading to
increased pH

19
BOHR EFFECT
• Increased CO2 helps to release more
Oxygen from the Haemoglobin.
• How?
• By altering the configuration and
decreasing the Oxygen affinity.
• Is useful during physical exercise when
more of Carbon dioxide is produced.
pH and PCO2: Bohr effect

21
Carbon Dioxide Transport
Method Percentage
• Dissolved in Plasma 7 - 10 %
• Chemically Bound to
Hemoglobin in RBC’s 20 - 30 %
• As Bicarbonate Ion in
Plasma 60 -70 %

Dissolved
bound to Hb
HCO3-

22
CARBON DIOXIDE IN THE
BLOOD
• CO2 crosses cell membranes much more
readily than O2.
• It needs to be transported out to the lungs
and thus into the external environment.
• It plays a vital role in maintaining body
fluids at their correct pHs: Acid Base
balance.(HOMEOSTASIS)
CARBON DIOXIDE IN PLASMA
• CO2 is more soluble than O2 in water.
• CO2 unlike O2 reacts with water.
• CO2 + H2O  H2 CO3 (Carbonic Acid)
• Carbonic Acid dissociates to Hydrogen &
Bicarbonate ions.
• H2 CO3  H+ + HCO3-
CARBON DIOXIDE IN PLASMA
• If the PCO2 increases, more CO2 dissolves
and the concentrations of H+ & HCO3
increase.
• On the other hand, if the [H+] & [HCO3]
levels rise, the CO2 will rise.
• The dissolved CO2 will be given out as gas.
• So, [H2CO3]  [H+] + [HCO3-]
CARBON DIOXIDE IN BLOOD

• 200 ml of CO2 is produced per minute at rest.


• It diffuses from the tissues to the blood.
• As it is more soluble, is more dissolved in
blood.
CARBON DIOXIDE IN BLOOD
• In physical solution Plasma/Erythrocyte:
10%
• As Carbamino Hemoglobin : 30%
– CO2 + Hb  HbCO2
• As Bicarbonate ions: 60%
– Mostly in the Erythrocyte which has the
enzyme, Carbonic anhydrase.(Catalyses the
formation of Carbonic acid 5000 times.)
– CO2 + H2O  H2 CO3 [H+] + [HCO3-]
CHLORIDE SHIFT
• Most of the HCO3- so formed in the
Erythrocyte, shifts out through a
transporter.
• This is an antiport which influxes one ion
of Chloride for every ion of Bicarbonate
shifting out.
• This is called as the Chloride shift or the
Hamburger Phenomenon/shift.
HAMBURGER EFFECT
• The Chloride shift occurs in the
tissue capillaries.
• Since some bicarbonate and Cl-
remain and the osmolarity of RBCs
increases, they swell slightly.
• This is called “Hamburger effect.”
THE CHLORIDE SHIFT

ERYTHROCYTE

CO2  CO2

CO2 + H2O  H2CO3

H+
+
HCO3- HCO3-
Cl-  Cl-
CO2 Transport and Cl Movement
-

31

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