Given the oxygen dissociation curves, which of the following statements are correct?Which residue in HbA β do you think contributes the most to the increased interaction between HbA aand 2,3‑BPG? HbFHbA + 2.5 mM BPG1.0Given the oxygen dissociation curves, which of theHbAНЬF +following statements are correct?2.5 mM BРG0.8`HbA lysateO Purified HbA has a higher oxygen affinity thanpurified HbF.0.62,3-BPG is an allosteric activator of HbA.The allosteric effects of 2,3-BPG are homotropic.0.42,3-BPG only weakly interacts with HbF.HbF loads oxygen at lower pO, than does HbA in the0.2presence of 2,3-BPG.0 103040506070pO, (torr)The researcher obtains the sequence used to generate the recombinant HbF and also sequences her sample of purified HbA.Knowing that the HbA ß subunit C-terminus is important for the interaction between HbA and 2,3-BPG, the researchercompares this portion of HbA with the C-terminal portion of the HbF y subunit.Primary sequence dataНЬА В136GVANALAHKYH146HbF Y136AVASALSSRYH146The structure of 2,3-BPG is shown.Which residue in HbA ß do you think contributes themost to the increased interaction between HbAaand 2,3-BPG?2-201/0, Which residue in HbA ß do you think contributes themost to the increased interaction between HbAaand 2,3-BPG?Lys-144His-143Asn-139Ala-142Gly-136

The binding of the oxygen molecule to a protein especially for transport or storage is known as…

HbF HbA + 2.5 mM BPG 1.0 Given the oxygen dissociation curves, which of the HbA, HbF + following statements are correct? 2.5 mM BPG 0.8 HbA lysate O Purified HbA has a higher oxygen affinity than purified HbF. 0.6 2,3-BPG is an allosteric activator of HbA. The allosteric effects of 2,3-BPG are homotropic. 0.4 2,3-BPG only weakly interacts with HbF. HbF loads oxygen at lower pO, than does HbA in the 0.2 presence of 2,3-BPG.

HbF HbA + 2.5 mM BPG 1.0 Given the oxygen dissociation curves, which of the HbA, HbF + following statements are correct? 2.5 mM BPG 0.8 HbA lysate O Purified HbA has a higher oxygen affinity than purified HbF. 0.6 2,3-BPG is an allosteric activator of HbA. The allosteric effects of 2,3-BPG are homotropic. 0.4 2,3-BPG only weakly interacts with HbF. HbF loads oxygen at lower pO, than does HbA in the 0.2 presence of 2,3-BPG.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 17P

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