Functional studies of the double mutant hemoglobin Stanleyville II/S α278 Lys β26 Val: Identification of a site of intermolecular contact on the α chain-Reference-Cited by-同舟云学术

Functional studies of the double mutant hemoglobin Stanleyville II/S α278 Lys β26 Val: Identification of a site of intermolecular contact on the α chain

Published:1977-08 Issue:3 Volume:77 Page:1108-1117
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Hassan W.,Beuzard Y.,North M.L.,Rosa J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. α-Chain contacts in the polymerization of sickle haemoglobin

2. Structure and Properties of Hemoglobin Carlem, a Human Hemoglobin Variant with Amino Acid Substitutions in 2 Residues of the β-Polypeptide Chain

3. Characterization of α23GluNH2in Hemoglobin Memphis. Hemoglobin Memphis/S, a New Variant of Molecular Disease*

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2. Hb Stanleyville II [alpha 78(EF7) Asn→Lys] occurrence in combination with Hb Constant Spring;Blood Cells, Molecules, and Diseases;2011-02-15

3. Sickle cell hemoglobin fiber formation strongly inhibited by the stanleyville II mutation (α78 Asn → Lys);Biochemical and Biophysical Research Communications;1983-02

4. Molecular topology in crystals and fibers of hemoglobin S;Journal of Molecular Biology;1981-08

5. Effect of Some physical Features and of Amino acid Substitutions on the Mechanical Precipitation of Hemoglobin;Hemoglobin;1981-01