The right of the oxygen dissociation curve shifted in:
(pH4): Ref: 593-H, 581-SL, 667-G, 468-GTN (611- Ganong 23rd)* Fetal haemoglobin (HbF) does not bind, 2, 3 D PG, so it tends to have a higher oxygen affinity in vivo, the oxygen hemoglobin curve shifted to left:Right side shift of oxygen - hemoglobin dissociation curve - causes1. Increased CO2 concentration2. Increased temperature (Hyperthermia)3. Increased 2,3 DPG, DPG is a by product in EMP-pathway of carbohydrates metabolism. It is present in RBC, in conditions like muscular exercise and in high altitude, the DPG increased in RBC, so the oxygen, hemoglobin dissociation curve shifts to right to a great extent4. Decrease in partial pressure of oxygen5. Increase in hydrogen ion concentration and decrease in pH (Acidosis)6. In anemia, curve is shifted to right side (56-SL)Left side shift of oxygen-hemoglobin dissociation curve1. In fetal blood-because fetal hemoglobin has got more affinity for oxygen than the adult hemoglobin2. Decrease in H+ concentration and increase in pH (Alkalosis)3. Hypothermia4. Blood transfusion: - In stored blood, the 2,3DPG levels falls and the ability of this to release 02 to the t issue is reduced, this leads to curve shift to left side* The decrease in 2,3DPG can be prevented by adding substance such as inosine (hypoxanthine-ribose) to storage medium (32- Lippancott's 2nd)
Fetal hemoglobin |
2,3 DPG|
pH |
Temperature |
Respiratory System