Blood composition changes as it passes thru the lungs, gas exchange at the alveoli.
Blood coming from Pulmonary Artery:
Oxygen: 40mmHg
Carbon Dioxide: 47mmHg
Blood coming from lungs into pulmonary vein:
Oxygen: 100mmHg
Carbon Dioxide: 40 mmHg
Arterial blood:Blood from pulmonary arteries with bronchial veins and left ventricle.Oxygen: 95mmHgCarbon Dioxide: 40 mmHg
Blood Oxygen Transport
Nota:
Dissolved and carried in blood in 2 forms:
Dissolved
Combined with haemoglobin
Haemoglobin
Nota:
Molecular weight of 64450KDs, 4 subunits which also consists of a haem molecule connected in a polypeptide chain.
2 alpha chains (141aa) and 2 beta chains (146 aa)
The haem molecule consists of a porphyrin derivatiive and one atom of Ferrous Fe2+.
Quarternary Structure
Nota:
Quarterany structure aids in loading of the oxygen molecules.
Available in 2 states
Tense and Relaxed.
It is also allosteric.
I.e when one molecule binds, it enables the other molecules to bind to them easier.
Oxygen capacity, saturation and content
Nota:
3 terms to remember:
Oxygen Capacity:
Amt of o2 which can combined with Hb. at normal its 15g/100ml.
Oxygen Saturation:
Percentage of available binding sites for Hb to attach.
Saturation Formula: O2 with Hb/O capacity X 100
Oxygen Content:
Amt of molecular oxygen that is released after destroying binding power of Hb.
Equation to determine O2 content
Nota:
(1.34 X Hb X Sat/100)+ 0.003 X Partial Pressure Oxygen
Saturation is 97.5% for normal Hb
1.34 is constant for Hb
0.003 is the solution constant for Oxygen
Hb-O2 equilibrium curve
Nota:
Important factors that shift the curve to the right.
increase in H conc i.e pH decreases
Increases in temperature
Increases in carbon dioxide conc
increase in 2,3 diphosphoglycerate (2,3 DPG)
notable points
Partial pressure of oxygen vs % Saturation
0 vs 0
20 vs 35
27 vs 50
40 vs 75
100 vs 97.5
Flat upper portion shows the o2 loading of the lungs
The steep lower portion shows the o2 diffusion into the tissues.
Bohr Effect
Nota:
Shift the OEC due to the change in blood pH and Co2.
hydrogen ions bind to the histidine residues on Hb and hence initiates conformational changes and it decreases affinity towards oxygen
This leads to enhanced oxygenation of blood in the lungs and release of oxygen in tissues.
2,3 DPC
Nota:
Produced by glycolysis of RBC
binds to deoxyHB therefore decrease affinity of oxygen binding.
Haemoglobin vs Myoglobin
Nota:
Different type, oxygen storage in muscle.
Binds to one oxygen
CO poisoning
Nota:
CO has higher affinity to Hb.
Forms carboxylhaemoglobin.
Symptoms of patient will be hypoxic. But no cyanosis.
COHb will be cherry red in color.