You repeat the experiment comparing the affinity of stripped

You repeat the experiment comparing the affinity of stripped and physiological hemoglobin but now in a solution that has high concentration of Cl-. You find that the presence of these ions shifts the stripped hB affinity curves to the right. Explain this phenomenon.

Solution

Oxygen plays a vital role in Haemoglobin\'s behaviour. Now , as affinity of haemoglobin to O₂ gradually increases more quantity of O₂ gets bound to haemoglobin . There occurs a sigmoidal shape to explain the graphical representation of the disassociation curve which predominantly demonstrates that how haemoglobin is co-operative to O₂ .

Let me first describe the left shift- when left shift takes place it indicates a greater O₂ affinity , thus haemoglobin easily bound to O₂ . In this case low temperature ,greater pH & reduce metabolism rate are the featured conditions.

Now, the right shift which is of prime concern in this question when right shift takes place it indicates a reduction in affinity , thereby heamoglobin has a greater chance to release O₂ . This scenario depends on high temperature , minimal pH & greater metabolism.