Essentials of Human Anatomy & Physiology (12th Edition)
Essentials of Human Anatomy & Physiology (12th Edition)
12th Edition
ISBN: 9780134395326
Author: Elaine N. Marieb, Suzanne M. Keller
Publisher: PEARSON
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Chapter 2, Problem 45CT
Summary Introduction

To analyze:

The change in one amino acid could affect hemoglobin function.

Introduction:

The hemoglobin is a multi-subunit protein that carries the oxygen throughout the body via red blood cells (RBCs). Sickle cell anemia (SCA) is a condition in which the shape of the hemoglobin is changed and so, its function is altered. The genetic error that causes SCA begins at the DNA (deoxyribonucleic acid) level. Thus, the synthesized hemoglobin has one amino acid difference as compared to the normal hemoglobin.

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sickle hemoglobin when deoxygenated will create a long line of protein cells? is this true? Please explain your answer. thanks
Sickle cell anemia is associated with which of the following:   Question 27 options:   Sticky patches on the hemoglobin surface only present in the T-state   Sticky patches on the hemoglobin surface only present in the R-state   A mutant form of hemoglobin called Ɣ-hemoglobin   Decreased ability to stabilize the T-state with 2,3-bisphosphoglycerate   Decreased ability to bind heme because of the Bohr effect
Hemoglobin glycation (so named to distinguish it from glycosylation, which is the enzymatic transfer of glucose to a protein) is a non-enzymatic process that involves reaction of the N-terminal amino group of hemoglobin and glucose. The amount of glycated hemoglobin (GHB) is usually about 5% of total hemoglobin (and corresponds to a blood glucose concentration of 120 mg/100 mL). However, in people with untreated diabetes this value may be as high as 13%, which indicates an average blood level of about 300 mg/100 mL -dangerously high. One of the aims of insulin therapy is to maintain GHB values of about 7%. Draw a possible chemical scheme for the glycation of hemoglobin.

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Essentials of Human Anatomy & Physiology (12th Edition)

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