1. Section 3 Gas Transport in the Blood

2. Basic Mechanism of the Gases Transportation
Two forms of the gases: physical dissolution and chemical combination.
Most of oxygen and carbon dioxide in the blood is transported in chemical combination
Only the gas in physical dissolution express PP and diffuse to a place with low PP.
Dynamic balance between the two forms:
Physical dissolution Chemical combination PP PP

3. I. Transport of Oxygen

4. Oxygen Transport Method Percentage Dissolved in Plasma 1.5 %
Combined with Hemoglobin %

5. Oxygen

6. Hemoglobin Structure
Hemoglobin is a protein made up of 4 subunits, each of which contains a heme moiety attached to a polypeptide chain.

7. Oxyhemoglobin Formation
Oxyhemoglobin forms when an oxygen molecule reversibly attaches to the heme portion of hemoglobin. The heme unit contains iron ( +2 ) which provides the attractive force. The process is summarized as follows:
O2 + Hb
HbO2

8. In normal adults, most of the hemoglobin contains 2α and 2 β chains
In normal adults, most of the hemoglobin 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 hemoglobin 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.

9. 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 O2 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: The percentage of all the available heme binding sites saturated with oxygen is the hemoglobin oxygen saturation

10. The oxygen-hemoglobin dissociation curve:
the curve relating percentage saturation of the O2-carry power of hemoglobin to the PO2.

11. The oxygen-hemoglobin dissociation curve
A. Flattened upper portion
B. Steep middle portion
C. Lower portion

12. Shifting the Curve

13. Factors that Shift the Oxygen-Hemoglobin Dissociation Curve

14. 1. PH and PCO2: Bohr effect

15. 2. Temperature

16. 3. 2,3-diphosphoglycerate, 2,3,-DPG (2, 3-二磷酸甘油）
A byproduct of anaerobic glycolysis.
Present in especially high concentration in red blood cells because of their content of 2,3-DPG mutase.
The affinity of hemoglobin for O2 diminishes as the concentration of 2,3-DPG increase in the red blood cells.

17. Importance:
The normal DPG in the blood …
Hypoxic condition that last longer than a few hours…
Disadvantage:
The excess DPG also makes it more difficult for the hemoglobin to combines with O2 in the lungs.

18. 4. Effect of Carbon Monoxide (CO)
CO combines Hb at the same point as does O2, and can displace O2 from hemoglobin.
CO binds with about 250 times as much tenacity as O2.
Therefore, a PCO only a little greater than 0.4 mmHg can be lethal.

19. 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% COHb (carboxyhemoglobin).

20. 5. Fetal Hemoglobin Advantage
Increased O2 release to the fetal tissues under the hypoxic condition.

21. II Carbon Dioxide Transport
Method Percentage
Dissolved in Plasma %
Chemically Bound to
Hemoglobin in RBC’s %
As Bicarbonate Ion in
Plasma %

22. Carbon Dioxide

23. Carbaminohemoglobin Formation
Carbon dioxide molecule reversibly attaches to an amino portion of hemoglobin.
CO2 + Hb
HbCO2

24. Carbonic Acid Formation
The carbonic anhydrase stimulates water to combine quickly with carbon dioxide.
CO2 + H2 0
H2 CO3

25. Bicarbonate Ion Formation
Carbonic acid breaks down to release a hydrogen ion and bicarbonate.
H2 CO3
H HCO-3

26. CO2 Transport and Cl- Movement

27. Carbon Dioxide Dissociation Curve
Haldane effect
For any given PCO2, the blood will hold more CO2 when the PO2 has been diminished.
Reflects the tendency for an increase in PO2 to diminish the affinity of hemoglobin for CO2.

28. Mechanism of Haldane effect
Combination of oxygen with hemoglobin in the lungs cause the hemoglobin to becomes a stronger acid. Therefore:
The more highly acidic hemoglobin has less tendency to combine with CO2 to form CO2 Hb
The increased acidity of the hemoglobin also causes it to release an excess of hydrogen irons

29. Interaction Between CO2 and O2 Transportation
1. Bohr effect

30. 2. Haldane effect