A 35Cl−-NMR study of the singular anion-binding properties of dromedary hemoglobin-Reference-Cited by-同舟云学术

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A 35Cl−-NMR study of the singular anion-binding properties of dromedary hemoglobin

Published:1989-11 Issue:1 Volume:999 Page:12-18
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:

Lundberg Peter,Vogel Hans,Drakenberg Torbjörn,Forsén Sture,Amiconi Gino,Forlani Luciano,Chiancone Emilia

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference33 articles.

1. STRUCTURE AND MECHANISM OF HAEMOGLOBIN

2. Hemoglobin: Molecular, Genetic and Clinical Aspects;Bunn,1986

3. Allosteric Effects in Haemoglobin;Imai,1982

4. Interaction of hemoglobin with salts

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1. Control of Oxygen Affinity in Mammalian Hemoglobins: Implications for a System Biology Description of the Respiratory Properties of the Red Blood Cell;Current Protein & Peptide Science;2020-08-21

2. Physiological consequences of oxygen-dependent chloride binding to hemoglobin;Journal of Applied Physiology;2001-07-01

3. K+-Ribosome interactions determine the large enhancements of 39K NMR transverse relaxation rates in the cytoplasm of Escherichia coli K-12;Biochemistry;1995-01-01

4. The influence of Mg2+ on anion binding to sarcoplasmic reticulum membranes as detected by 35Cl-NMR;Biochimica et Biophysica Acta (BBA) - Biomembranes;1992-04

5. Nuclear magnetic resonance studies of cellular metabolism;Analytical Biochemistry;1990-12

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