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OXIGEN & CARBON DIOXIDE

TRANSPORT
Disusun Oleh:
Husnil Kadri
Biochemistry Departement
Medical Faculty Of Andalas
University

Oxygen Transport

Total Body Oxygen Stores


Oxygen in the Lung (~500 ml O2).
Oxygen in the Blood (~850 ml O2).
Oxygen in the Cells (very little except
Mb-bound).

AttheLungLevel

AttheTissueLevel

Two Forms Of Oxygen in Blood


Bound to hemoglobin in red blood cells.
Dissolved in plasma. Normally
insignificant.

Hemoglobin
Each heme molecule is capable of binding with
1 O2 molecule and each globin molecule is
capable of binding with 1 CO2 molecule.
So, each molecule of Hb can bind 4 molecules
of O2 and 1 molecule of CO2
100 ml of blood has about 15 gr of Hb, at Hct =
0.45

Binding of O2 to 4 heme sites given by:

Hb O2 HbO2
HbO2 O2 Hb(O2 ) 2
Hb(O2 ) 2 O2 Hb(O2 ) 3
Hb(O2 ) 3 O2 Hb(O2 ) 4
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Oxygen as Oxyhemoglobin
Each gram of Hb can store about 1.34 ml
of O2:
1 L of blood (150 gr of Hb) can store about
208 ml of O2 Oxygen Capacity of Hb.
With normal cardiac output, about 1040 ml
of O2 can be carried in blood per minute. (4
times of the metabolic demands).

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O2 Saturation.
Units: percent.
Fraction or percentage of all the
hemoglobin binding sites that are
currently occupied by oxygen.

Oxygen Saturation of Hb
O 2 combined with Hb
SHbO2 (% saturation)
100
O 2 capacity of Hb

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Four (5-6?) Things Change


Oxyhemoglobin Affinity
1. Hydrogen Ion Concentration, [H +]
2. Carbon Dioxide Partial Pressure, PCO 2
3. Temperature
4. 2,3 diphosphogliceride [2,3-DPG]
5. Special Case: Carbon Monoxide
6. Hemoglobin variants

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Factors Affecting Hb-O2 Affinity:


Summary
Hydrogen Ion:
Increased H+ (decreased pH) increases H+ binding to Hb
and reduces O2 affinity (HbO2+H+HbH++O2).

Carbon Dioxide (Bohr effect):


Increased PCO2 increases CO2 binding to Hb and reduces
O2 affinity (increased O2 delivery to tissue).
Increased PCO2 increases H+ and reduces O2 affinity
(fixed acid Bohr effect).

Temperature and 2,3-DPG (diphosphoglycerate):


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Increased temperature and 2,3-DPG reduces O 2 affinity.

Effect of CO & Anemia on Hb-O2 Affinity

Normal blood with Hb=15 gm/dl, anemia with Hb=7.5 gm/dl,


and normal blood with 50% HbCO (carboxyhemoglobin).

Exercise
Increase temperature
Increased PCO2 and
Decreased pH (acidosis)

2,3-DPG
2,3-DPG is a glycolytic intermediate
accumulates to uniquely high levels in RBCs
-Increased 2,3-DPG
-Decreased 2,3-DPG

right shift
left shift

Conditions with Increased 2,3-DPG

acclimatization to high altitudes.


chronic lung disease; emphysema.
anemia.
hyperthyroidism.
right to left shunt.
congenital heart disease.
pulmonary vascular disease.

Carbon Dioxide
Transport

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AttheTissueLevel

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AttheLungLevel

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Carbon Dioxide Transport


CO2 is transported in blood in dissolved form, as
bicarbonate ions, and as protein-bound carbamino
compound.

Amount of CO2 stored as carbamino compounds


is about 21 ml/L (4% of the total art CO2).

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Carbon Dioxide Transport


A majority amount of CO2 is transported in the
form of bicarbonate ions (HCO3-):
CO 2 H 2O CA H 2CO3
H HCO-3

Amount of CO2 in HCO3- form at PCO2=40


mmHg is about 420 ml/L (90% of the total
arterial CO2).

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Carbon Dioxide Transport


Haldane Effect: Increasing O2-saturation reduces
CO2 content and shifts the CO2 dissociation
curve to right. This is because, increasing P O2
leads to :
Decrease in the formation of carbamino compound.
Release of H+ ions from the hemoglobin and resulting
in dehydration of HCO3-.

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Carbon Dioxide Dissociation Curve

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Bicarbonate in RBCs.
Carbonic anhydrase is present in RBCs
CO2 forms carbonic acid which
dissociates to H+ and HCO3CO 2 H 2 O

H 2 CO 3
H HCO 3

Carbonic Anhydrase

PercentofthetotalPaCO2:70%

Carbamino Compounds in RBCs.


Approximately 30% of RBC contents is Hb
CO2 forms carbamino hemoglobin

PercentofthetotalPaCO2:23%

CO2 Formation in Plasma


Carbamino compounds
CO2 binds the amine groups of plasma
proteins to form carbamino compounds.
R NH 2 CO2 R NH COO H

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Chloride Shift (Hamburger Shift)


Newly formed HCO3- passes out of RBC
Cl- diffuses into RBC to maintain
electroneutrality
Chloride shift is rapid
Complete before the RBCs exit capillary

Tissue-Gas Exchange: Summary


Gas exchange processes in the peripheral organs
are essentially opposite those in the lungs.
O2 is released from the capillary blood to the
tissues and diffuses to the mitochondria where O 2 is
converted to CO2 and energy (ATP) through cellular
metabolism.

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References

BIOEN
589:
Integrative
Physiology.
Download
24 jan 05.
Kennelly, PJ., Rodwell, V W. Proteins: Myoglobin & Hemoglobin. In:
Harpers Illustrated Biochemistry. 27th Ed. 41- 8.
Miliefsky, M. Respiratory System Ch.23. Download 24 Nov 10.
Sheardown, H. Blood Biochemistry. McMaster University. Download
20 Mei 07.
Irvin, CG. Respiratory Physiology. Lecture 4A CO2 Transport. In:
MEDICAL PHYSIOLOGY 30. Download 22 Jun 09.
Marks, DB., Marks, AD., Smith CM. Basic medical biochemistry: a
clinical approach. 1996. Dalam: B.U. Pendit, penerjemah. Biokimia
Kedokteran Dasar: Sebuah Pendekatan Klinis. Eds. J. Suyono., V.
Sadikin., L.I. Mandera. Jakarta: EGC, 2000
R.K. Murray, D.K. Granner, P.A. Mayes, V.W. Rodwell Harpers
Biochemistry. 27th ed. McGraw-Hill Companies, New York. 2006.

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