CO(Carbon monoxide) completely binds to Hb at oxygen binding site and is toxic T

Question

CO(Carbon monoxide) completely binds to Hb at oxygen binding site and is toxic True False Mb and Hb exhibit similar behavior toward O_2 binding. True False Need more information "Bohr effect" refers to the ability of hemoglobin to retain oxygen when in competition with myoglobin. The regulation of O_2 binding to hemoglobin by H^+ and CO_2. The alteration of hemoglobin conformation during low oxygen stress. All of the above. None of the above. Sickle-cell anemia is caused by a mutation in the gene encoding Hb. a substitution of a Glu residue for a the residue at the beta6 position. the loss of the home group because the proximal His is oxidized. modifications in the alpha subunit. a substitution of Glu residue for His at the C-terminal of the alpha chain. Which of the following is correct concerning the oxygenation plot of proteins X and Y shown below? Protein Y exhibits tighter oxygen binding than protein X. Protein Y would function as a better storage protein of O2 than protein X. Protein Y exhibits cooperative binding, whereas X does not. Protein X corresponds to hemoglobin, and protein Y corresponds to myoglobin

Explanation / Answer

4 ) True

5) False

Mb ahs higher affinity for O2 binding than Hb.

6) E - none

The Bohr Effect refers to the observation that increases in the carbon dioxide partial pressure of blood or decreases in blood pH result in a lower affinity of hemoglobin for oxygen.

7) A

Sickle cell anemia is caused by a mutation in the gene that tells our body to make hemoglobin — the red, iron-rich compound that gives blood its red color.

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