HUMAN HEREDITY (LL)-W/MINDTAP ACCESS
11th Edition
ISBN: 9781305717022
Author: Cummings
Publisher: CENGAGE L
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Chapter 10.7, Problem 1EG
Summary Introduction
To explain: The way in which a single amino acid in beta globin chain can lead to sickle cell anemia.
Introduction: Sickle cell anemia is a genetic disease that is inherited from one generation to next in an autosomal recessive manner. People suffering from this disease show mutations in the genes that code for the β-globin chain of hemoglobin. This results in the formation of improperly folded hemoglobin molecule. Red blood cells of people suffering from this disease are sickle shaped..
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The group of disorders associated with single gene mutations affecting amino acid sequences in the alpha and beta globin genes are called
Question 10 options:
A)
thalassemias
B)
hemoglobinopathies
C)
hemolytic anemias
D)
megaloblastic anemias
Name the base change and aminoacid change,responisble for sickle-cell anemmia?
Name the base change and the amino acid change, responsible for sickle cellanaemia.
Chapter 10 Solutions
HUMAN HEREDITY (LL)-W/MINDTAP ACCESS
Ch. 10.4 - Prob. 1GRCh. 10.4 - Prob. 2GRCh. 10.7 - Prob. 1EGCh. 10.7 - Prob. 2EGCh. 10 - A couple was referred for genetic counseling...Ch. 10 - A couple was referred for genetic counseling...Ch. 10 - A couple was referred for genetic counseling...Ch. 10 - Many individuals with metabolic diseases are...Ch. 10 - Prob. 2QPCh. 10 - Enzymes have all the following characteristics...
Ch. 10 - Questions 4 through 6 refer to the following...Ch. 10 - Questions 4 through 6 refer to the following...Ch. 10 - Prob. 6QPCh. 10 - Prob. 7QPCh. 10 - Prob. 8QPCh. 10 - a. Compounds A, B, C, and D are known to be...Ch. 10 - b. Compounds A, B, C, and D are known to be...Ch. 10 - a. If an individual who is homozygous for the...Ch. 10 - Prob. 12QPCh. 10 - Suppose that in the formation of phenylalanine...Ch. 10 - If phenylalanine was not an essential amino acid,...Ch. 10 - Phenylketonuria and alkaptonuria are both...Ch. 10 - The normal enzyme required for converting sugars...Ch. 10 - Knowing that individuals who are homozygous for...Ch. 10 - Prob. 18QPCh. 10 - A person was found to have very low levels of...Ch. 10 - If an extra nucleotide is inserted in the first...Ch. 10 - Transcriptional regulators are proteins that bind...Ch. 10 - Prob. 22QPCh. 10 - Prob. 23QP
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- Where is beta globin gene?arrow_forwardWhat is BCL11A and how is it related to hemoglobin?arrow_forwardIn 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 O B) A change in the oxygen binding to hemoglobin that causes formation of polymers C) Changes in the interaction between B-chains and x-chains OD) Changes in binding of 2,3-bisphosphoglyceratearrow_forward
- How is hemolytic anemia related to pentose phosphate?arrow_forwardUse the image below to answer this question and the three questions that follow: a) what is the correct description of the hemoglobin for Paul? b) Where is the + pole of the electrophoresis for the gel shown in the previous question? c) Refer to gel illustration above. Which of the following statements provides the best explanation for the difference in mobility of HbA and HbS? 1) HbA is larger in size than HbS 2) HbA is smaller in size than HbS 3) HbA has less negative charge than HbS under electrophoretic conditions used 4) HbA is smaller and more negatively charged under the electrophoretic conditions used 5) HbA is larger and has a less negative charge under the electrophoretic conditions used, whereas HbS is smaller and has a more negative chargearrow_forwardWhy does the immune system recognize particular sugars on red blood cells?arrow_forward
- What is oxyhemoglobin? Where does it form?arrow_forwardIn sickle cell anemia, hemoglobin forms long fibers as a result of a) Burying of non-polar amino acids b) Burying polar amino acids c) Exposing polar amino acids d) Electrostatic interaction between glutamate and non polar amino acidsarrow_forwardGlucose reacts slowly with hemoglobin and other proteins to form covalent compounds. Why is glucose reactive? What is the nature of the adduct formed?arrow_forward
- 1. a) True or False - A mutation in the beta globin gene that causes conversion of His146 to Glutamate would decrease Hemoglobin’s O2 binding affinity. b) True or False - A mutation in the beta globin gene that causes conversion of His146 to Glutamate would eliminate Hemoglobin’s positive cooperativity.arrow_forwardWhich of these statements about hemoglobin is NOT true? A) it is a tetrameric globular protein b) it has a prosthetic group called heme c) it’s dominant motif is beta barrel d) its dominant motif is helix-turn-helix The reagent used to break disulfide bonds is: a) urea b) beta-mercaptoethanol c) guanidine hydrochloride d) phosphorus pentachloridearrow_forwardFetal hemoglobin comprises of αγ sub-units. It has been found that the γ-chain contains serine at position 143 instead of Histidine 143 normally found in the β-chain. The amino acid 143 lines the DPG binding site. This mutation in the γ chain results in a) Increased Oxygen binding in the fetus. b) Increased efficiency of oxygen transport to the lungs in the fetus. c) Increased DPG binding in the fetal hemoglobin d) This is a silent mutation, i.e. no change should be observed.arrow_forward
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