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Topic: mutant hemoglobin  (Read 5414 times)

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Offline aj3537

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mutant hemoglobin
« on: September 22, 2008, 09:07:23 PM »
This is a Homework question. I have answered it and want to know it its right or if there is more to it.

Predict the effect on oxygen transport of a mutant form of hemoglobin with a markedly decreased affinity for glycerate-2,3-bisphosphate.

Hemoglobin interacts with 2,3-bisphosphoglycerate to significantly lower hemoglobin’s oxygen affinity. Therefore, if the mutant hemoglobin can’t bind to 2,3-bisphosphoglycerate, the affinity for oxygen  greatly increases. This means that oxygen will bind to hemoglobin easier and makes it harder for oxygen to leave the hemoglobin.

Offline Yggdrasil

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Re: mutant hemoglobin
« Reply #1 on: September 23, 2008, 01:17:04 AM »
What are the 2,3-BPG concentrations in the lungs relative to the rest of the body's cells?  How does this influence oxygen transport?

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