Allosteric properties of haemoglobin β41 (C7) Pheå Tyr: a stable, low-oxygen-affinity variant synthesized in Escherichia coli-Reference-Cited by-同舟云学术

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Allosteric properties of haemoglobin β41 (C7) Pheå Tyr: a stable, low-oxygen-affinity variant synthesized in Escherichia coli

Published:1992-09 Issue:2 Volume:1159 Page:223-226
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Baudin Véronique,Pagnier Josée,Lacaze Nicole,Bihoreau Marie-Thérèse,Kister Jean,Marden Michael,Kiger Laurent,Poyart Claude

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference17 articles.

1. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

2. NMR study of Human Mutant Hemoglobins Synthesized in Escherichia coli

3. Site-directed mutagenesis in haemoglobin

4. Hemoglobin M equon beta 41 (C7) phenylalanine leads to tyrosine

5. Generation of β-globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli

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2. Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation;Journal of Biological Chemistry;2019-03

3. Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design;Biochemical Journal;2016-09-27

4. Interaction of recombinant octameric hemoglobin with endothelial cells;Comptes Rendus Biologies;2015-02

5. Hb Octamers by Introduction of Surface Cysteines;Chemistry and Biochemistry of Oxygen Therapeutics;2011-07-04

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