Question

What is the effect of the following changes on the O2 affinity of hemoglobin?

(a) An increase in the pH of blood plasma from 7.4 to 7.8.
(b) An increase in the partial pressure of CO2 in the lungs from 2 kPa (normal) to 6 kPa (holding one’s breath).
(c) A decrease in the BPG level from 8 mM (high altitudes) to 5 mM (normal altitude).
(d) An increase in CO from 1.0 parts per million (ppm) in a normal indoor atmosphere to 30 ppm in a home that has a malfunctioning or leaking furnace

Answer 1

Answer and Explanation:

The affinity of hemoglobin for Oxygen is controlled when the ligands $H^{+}$ , $CO_{2}$ and BPG binded.

The binding of every ligand moves the saturation curve of  Oxygen towards right—that is, the oxygen affinity of hemoglobin is decreased within the sight of ligand.  

(a) A pH drop will expand the oxygen affinity to myoglobin and decline the oxygen affinity for hemoglobin. This implies less oxygen will be taken by the lungs and more will be off stacked at the tissues diminishes the affinity.

(b) An abatement in the partial pressure of $CO_{2}$ will expand affinity of oxygen to hemoglobin and diminishes the affinity of oxygen for myoglobin expands the affinity.

(c) An expansion in BPG levels diminishes the affinity of oxygen for hemoglobin and expands oxygen's affinity for myoglobin  diminishes the affinity.  

(d) As CO ties to a couple of subunits of a hemoglobin tetramer, the affinity for oxygen is expanded generously in the rest of the subunits. Subsequently, a hemoglobin tetramer with two bound CO particles can productively tie oxygen in the lungs—yet it discharges almost no of it in the tissues.