Part 4 Oxygen and Carbon Dioxide Transport in Blood

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Part 4 Oxygen and Carbon Dioxide Transport in Blood

Physical dissolution Chemical combination Basic Mechanism Two forms of the gases: physical dissolution and chemical combination. Most of O2 and CO2 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

I. Transport of Oxygen

Oxygen Transport Method Percentage Dissolved in Plasma 1.5 % Combined with Hemoglobin 98.5 %

Oxygen

Hemoglobin Structure Protein made up of 4 subunits Every subunit contains a heme moiety attached to a polypeptide chain.

Oxyhemoglobin Formation An oxygen molecule reversibly attaches to the heme portion of hemoglobin. The heme unit contains iron ( +2 ) which provides the attractive force. O2 + Hb HbO2

Basic Concepts: Oxygen Capacity (氧容量): The maximum quantity of oxygen that will combine chemically with the hemoglobin in a unit volume of blood Normal Value: 1.34 ml of O2 per gm of Hb or 20 ml of O2 per 100 ml of blood. Oxygen Content(氧含量): how much oxygen is in the blood Oxygen Saturation (血氧饱和度): The percentage of all the available heme binding sites saturated with oxygen

The oxygen-hemoglobin dissociation curve: (氧离曲线) the curve relating percentage saturation of the O2-carry power of hemoglobin to the PO2.

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

Shifting the Curve

Factors that Shift the Oxygen-Hemoglobin Dissociation Curve

1. pH and PCO2: Bohr effect

2. Temperature

3. 2,3-diphosphoglycerate, 2,3,-DPG (2, 3-二磷酸甘油) A byproduct of anaerobic glycolysis. Present in high concentration in red blood cells because of their content of 2,3-DPG mutase (变位酶). Diminishes the affinity of hemoglobin for O2

Importance: 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.

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. PCO greater than 0.4 mmHg can be lethal. In the presence of CO (low concentration), the affinity of hemoglobin for O2 is enhanced

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

II 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 %

Carbon Dioxide

Carbaminohemoglobin (氨基甲酰血红蛋白) Formation Carbon dioxide molecule reversibly attaches to an amino portion of hemoglobin. CO2 + Hb HbCO2

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

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

CO2 Transport and Cl- Movement

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.

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

Interaction Between CO2 and O2 Transportation 1. Bohr effect

2. Haldane effect