Answer and Explanation:
The affinity of hemoglobin for Oxygen is controlled when the ligands ,
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 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.