Circle the correct terms Increased 2 3BPG Increased CO2 Incr

Circle the correct terms. Increased [2, 3-BPG] Increased [CO2] Increased [H+] Animals live in high altitude Patient with sickie cell anemia

Solution

Increased (2,3-BPG), the most stable form of heamoglobin will be T form. It binds to thecavity of deoxy-conformation, exploiting the symmetry of the molecule and forms the salt bridge between lysine and histidine in beta subunit of the heamoglobin. When in the R state, oxygen is bound to the heamoglobin so it remains in different conformation and does not allow the interaction. As it binds to heamoglobin, oxygen will be released into nearby tissues. so, in increased (2,3- BPG) condition O2 release will also increases. Increased CO2, in the high concentraton of CO2, the stable form of heamoglobin is T form that is deoxygenated form and results in the release of Oxygen from it. Reason for this is, when CO2 bind to hemoglobin it stabilizes the T form, ultimately forms a carbamate group which is negatively charged and these negatively charged molecules forms the salt bridge. Due to this, T state is stabilized and release the oxygen from heamoglobin. In this way higher the concentration of CO2, higher O2 release. Increased H+ ion concentration will result in lowring the pH which in turn cause the protonation of histidine residues and the salt bridge is formed between histidine and aspartate of hemoglobin. This causes the stabilization of T state of heamoglobin and thus high release of O2 from hemoglobin. In animals who live in high altitude, the affinity of hemoglobin towards oxygen becomes high, therefore it tends to remain stable in R state. And as the hemoglobin affinity is higher towards oxygen, the release of O2 from the hemoglobin decreases that is low O2 release causes the hypoxia, the condition in which the oxygen supply to the tisuues is deprived. Red blood cells of patients with sickle cell anemia becomes sickle shaped instead of normal oval shape of hemoglobin. The aggregate of hemoglobin in RBCs causes its change of shape from oval to sickle shaped. Due to this aggregation, oxygen cannot enter hemoglobin and cannot bind with hemoglobin, thus poor carrying capacity and poor release of oxygen. In this disease, a valine residue lies upon the T state molecule which changes it into hemoglobin S. So we can say that it is in T state but due to aggregation oxygen cannot enter that aggregated fibre of hemoglobin and thus oxygen release is poor (low).