Reversible binding of hemoglobin to band 3 constitutes the molecular switch that mediates O2 regulation of erythrocyte properties-Reference-Cited by-同舟云学术

Reversible binding of hemoglobin to band 3 constitutes the molecular switch that mediates O2 regulation of erythrocyte properties

Published:2016-12-08 Issue:23 Volume:128 Page:2708-2716
ISSN:0006-4971
Container-title:Blood
language:en
Short-container-title:

Author:

Chu Haiyan¹^ORCID,McKenna Mary M.²,Krump Nathan A.²,Zheng Suilan¹,Mendelsohn Laurel³,Thein Swee Lay³,Garrett Lisa J.⁴,Bodine David M.²,Low Philip S.¹

Affiliation:

1. Department of Chemistry, Purdue University, West Lafayette, IN; and

2. Genetics and Molecular Biology Branch, National Human Genome Research Institute,

3. Sickle Cell Branch, National Heart, Lung, and Blood Institute, and

4. Embryonic Stem Cell and Transgenic Mouse Core Facility, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD

Abstract

Key Points The reversible association of deoxyHb with band 3 acts as an O2-triggered molecular switch to regulate erythrocyte properties. Transgenic mice lacking the deoxyHb site on band 3 fail to respond to changes in O2 with changes in erythrocyte properties.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Link

http://ashpublications.org/blood/article-pdf/128/23/2708/1397740/blood692079.pdf

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5. The erythrocyte as a regulator of vascular tone;Ellsworth;Am J Physiol,1995

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