11. Which of the following best describes what happens when hemoglobin bindsbisphosphoglyceric acid (BPG)?A. Binding of BPG leads to tighter binding of oxygen.B. Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.C. Binding of BPG is important to the allosteric nature of hemoglobinD. Binding of BPG causes the subunits of hemoglobin to separate.

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

Answered: 11. Which of the following best…

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

See similar textbooks

Similar questions

In mammals, the developing fetus obtains O₂ from its mother's blood via the placenta. For this to occur... A. The fetal hemoglobin must have a higher Pso than the maternal hemoglobin B. The O₂ equilibrium curve of the fetal hemoglobin must be left-shifted with respect to the curve for the maternal hemoglobin C. The maternal hemoglobin must have a higher O₂ binding affinity than the fetal hemoglobin D. The O₂ carrying capacity of the fetal hemoglobin must be greater than that of the maternal hemoglobin E. None of the above
8. With respect to hemoglobin, how do you think carbon monoxide can cause hypoxic (low- oxygen) tissue injury and eventually death?
1. Regarding Sickle Cell Disease all are correct except one ○ a. Occur in alpha haemoglobin ○ b. Results from a single amino acid substitution ○ c. An inherited blood disorder ○ d. Red blood cell can not carrying oxygen
Which of the following scenariosare correct?Select all that apply A. High levels of PCO2will cause loading of O2ontohemoglobin. B. An increase in pH will causeO2to unload from hemoglobin. C. High PO2levels will increase saturation of Hb with O2. D. An increase in bodytemperature will cause O2to unload from hemoglobin.
8. Researchers obtain a pure solution of antibodies that bind specifically to the cadherins (linking proteins) of the desmosomes of epithelial cells of a mouse. As a follow up of their previous experiment, they take a tube of individual muscle cells from a chicken and add antibodies to the tube. What is the predicted outcome of this second experiment? A. The antibodies will bind to the chicken muscle cells, so the cells will adhere to each other B. The antibodies will bind to the chicken muscle cells, so the muscle cells will not adhere to each other C. The antibodies will not bind to the chicken muscle cells, so the cells will adhere to each other D. The antibodies will not bind to the chicken muscle cells, so the cells will not adhere to each other
6. As the pH of its surrounding environment decreases from 7.4 to 7.0, protonation of particular in hemoglobin allows the formation of salt bridges that stabilize the quaternary structure, resulting in A. Fe2*; R; increased B. Asp; T; decreased C. Fe2*; T; increased D. His; R; increased E. His; T; decreased state of the oxygen-binding affinity.
Why is haptoglobin depletion the most sensitive indicator of hemolysis among plasma proteins? Because it ?? a. helps to separate hemoglobin from lysing red blood cells b. binds free hemoglobin dimers following lysis of red blood cells c. is synthesized in the liver that is involved in extravascular hemolysis d. helps to degrade hemoglobin into iron and amino acids (globin) in the Kupffer cells
MCQ joining of iron moieties on the globulin protein occur in the following part of cell. A. cytoplasm b. nucleus c.mitochondria d.cell membrane
Based on your understanding of genetic code,explain the formation of any abnormal hemoglobin molecule?
Identify the human form of hemoglobin that is produced most abundantly in the adult.A. two -globin chains (alpha) and two -globin chains (beta)B. two -globin chains (beta) and two -globin chains (gamma)C. two -globin chains (gamma) and two -globin chains (delta)D. two -globin chains (delta) and two -globin chains (epsilon)E. two -globin chains (epsilon) and two -globin chains (zeta)
5. Explain how the Bohr effect plays a role in oxygen transport in vivo. w 6. Identify the mutation(s) in hemoglobin that result in the genetic disorder sickle cell disease. Then, describe the effect of the mutation on the shape of red blood cells. Lastly, describe symptoms and treatments for the disease.
The Bohr effect related to A. the ability of Hb to bind 02 in the presence of BPG. the ability of myoglobin to expel protons when binding 02. B. the ability of Hb to "take up" protons when binding 02. C. the ability of Hb to release protons when binding O2. D. O E. BPG ionization at 30 torr (the pO2 in veins).

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS