In hemoglobin from patients with sickle cell anemia, the hemoglobin ß-chains have a single amino substitution that results in: A) A sticky spot in the hemoglobin causing polymerization B) A change in the oxygen binding to hemoglobin that causes formation of polymers C) Changes in the interaction between ß-chains and x-chains
In hemoglobin from patients with sickle cell anemia, the hemoglobin ß-chains have a single amino substitution that results in: A) A sticky spot in the hemoglobin causing polymerization B) A change in the oxygen binding to hemoglobin that causes formation of polymers C) Changes in the interaction between ß-chains and x-chains
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Sickle cell anemia is a genetic disease that results in the formation of the sickle shape of RBCs. The sickle shape of RBCs is a result of the precipitation of mutated beta-globin chains in sickle cell anemia patients. The precipitation of hemoglobin in the deoxygenated state is a result of the mutation of valine from aspartic acid in the beta-globin chain.
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