Effect of chloride ion on the oxygen affinity of hemoglobin York (alpha 2 beta 2(146)Pro) and S-York hybrid hemoglobin (alpha 2 beta S beta York). Role of the beta 82 lysyl and beta 146 histydyl residues in chloride binding to hemoglobin.-Reference-Cited by-同舟云学术

Effect of chloride ion on the oxygen affinity of hemoglobin York (alpha 2 beta 2(146)Pro) and S-York hybrid hemoglobin (alpha 2 beta S beta York). Role of the beta 82 lysyl and beta 146 histydyl residues in chloride binding to hemoglobin.

Published:1983-11 Issue:22 Volume:258 Page:13422-13424
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Adachi H,Asakura T,Adachi K

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Studies on the Relations between Molecular and Functional Properties of Hemoglobin

2. Oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration

3. Stabilizing Interactions in Hemoglobin

4. Nuclear magnetic resonance quadrupole relaxation studies of chloride binding to human oxy- and deoxyhaemoglobin

5. Nuclear magnetic resonance quadrupole relaxation study of chloride binding to hemoglobin abruzzo (α2Aβ2143 His → Arg)

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