Explanation The β chains of adults have a lesser affinity for oxygen as compared to the ε chains in the embryonic stage and the γ chains in the fetal stage. When the oxygen molecule binds to the hemoglobin, its conformation changes to oxyhemoglobin or the relaxed (R). When the oxygen is disassociated, it forms deoxygenated hemoglobin or the taut (T) state. The 2, 3-bisphosphoglycerate (BPG) has a higher affinity for the T-state of hemoglobin, as compared to the R-state...

Biochemistry: The Molecular Basis of Life

6th Edition

ISBN: 9780190209896

Author: Trudy McKee, James R. McKee

Publisher: Oxford University Press

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Question

Chapter 5, Problem 11Q

Summary Introduction

To review:

The consequences of the binding of hemoglobin to 2, 3-bisphosphoglycerate (BPG) for the mother and the fetus.

Introduction:

Hemoglobin is a globular protein found in the red blood cells of an individual. It performs the function of oxygentransport from the lungs to the other tissues of the body. There are four polypeptide chains: two α and two β chains, in case of adults. The β chains are replaced by ε chains in the embryonic stage and γ chains in the fetal stage.

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Chapter 5 Solutions

Biochemistry: The Molecular Basis of Life

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Solution Summary: The author explains the consequences of the binding of hemoglobin to 2, 3-bisphosphoglycerate (BPG) for the mother and the fetus.

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