1. (10) Hemoglobin Ohio is a mutant HB in which beta 142 (H20) Ala is replaced b

Question

1. (10) Hemoglobin Ohio is a mutant HB in which beta 142 (H20) Ala is replaced by Asp. Explain the following properties of the mutant protein. 1or2 sentences is enough. Ba ?2 BPG N+ N+ Pa a) The hemoglobin has high oxygen affinity. b) reduced Bohr effect c) divioished cooperativity. d) Patients have erythrocytosis, an abnormally high red blood cell count (this is not directly related to the hemoglobin protein structure but it is related to the problem e) what do you predict will happen to BPG binding. Don't google it, tell me what you think based on what you have learned in class

Explanation / Answer

Haemoglobin Ohio has the high oxygen affinity, reduced Bohr effect, diminished cooperativity and erythrocytosis condition this is basically because of conversion of Ala to Asp result in the less stable T state so more likely this haemoglobin is present in relaxed state inside the cell which has the high affinity to the oxygen. we all know that with the increase of the oxygen affinity there is the reduction in the Bohr effect and diminished cooperativity is mainly due to the less stable T state.

it is well known that oxygen affinity and the BPG binding have the inverse relationship, so with the increase of the oxygen affinity there will be decrease binding o the BPG

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