After exhalation of carbon dioxide, His 146 becomes in O Protonated; Increased O Deprotonated; Decreased oxygen binding affinity by hemoglobin. Deprotonated; Increased Protonated; Decreased resulting
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- Among the given statements. which ones are true for hemoglobin? Select the correct response(S). It has ferrous cation that is coordinated by the electrophilic N atoms of the porphyrin ring. It has 4 sub-units with each sub-unit binding an oxygen molecule with the same efficiency. It has 4 sub-units with each sub-unit binding an oxygen molecule in an increasing efficiency. It has ferric cation that is coordinated by the electrophilic N atoms of the porphyrin ring. It has 4 sub-units with each sub-unit binding an oxygen molecule in a decreasing efficiency. It has ferric cation that is coordinated by the nucleophilic N atoms of the porphyrin ring. It has 4 sub-units with each sub-unit binding an oxygen molecule in a fluctuating efficiency.It has ferrous cation that is coordinated by the nucleophilic N atoms of the porphyrin ring.Hemoglobin molecules exposed to high levels of glucose areconverted to glycated products. The most common, referred to as hemoglobin A1C (HbA1C), contains a b-chain glycatedadduct. Because red blood cells last about 3 months, HbA1Cconcentration is a useful measure of a patient’s blood sugarcontrol. In general terms, describe why and how HbA1Cforms.Allosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformation
- 2,3 BPG is an allosteric effector that decrease haemoglobin affinity for oxygen by stabilizing the T-state of deoxyhaemoglobin. This lead to the release of oxygen to cells and body tissues for use. H atom and CO2 are also allosteric effector and can do same. How?A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?Diagram the Embden-Meyerhof anaerobic glycolytic pathway (EMP) in the red blood cell (RBC), highlighting adenosine triphosphate (ATP) consumption and generation.
- O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr effect from the molecular perspective. Be sure to include discussion of what causes this (i.e. specific amino acids), why the curves are right shifted with decreasing pH, and why this is logical in delivery of 02 to areas of higher demand. 100 Myoglobin 80- pH 7.6 60 pH 7.4 pll 7.2 40- pH 7.0 pH 6.8 20- Venous 0- 0. 20 10 60 80 Percent saturationHemophilia B, an X-linked genetic disorder which highly affects males, is a condition in which levels of Factor VIII are significantly decreased. Please describe the physiologic pathway which utilizes Factor VIII and describe the consequences of missing this factor from a physiologic perspective.Pentose phosphate pathway and hemolytic anemia. Explain the relationship.
- If a person lacks the enzyme necessary for BPG synthesis, does he orshe exhibit anemia (a lower-than-normal number of red blood cells) orerythrocytosis (a higher-than-normal number of red blood cells)? Explain.The primary allosteric regulator of hemoglobin oxygen affinity is ( ) and functions by stabilizing the ( ) state of enzyme.A researcher, in a study involving acid-base properties of RBC's notices the resistance of change in pH, when a small amount of acid or base is added to it. Buffering action of hemoglobin in RBCS is most likely attributed to presence of which of the following factors in the globin chains? Alpha helical structures В Beta pleated sheets C Ferric state of iron D Ferrous state of iron E Histidine residues