Biochimica et Biophysica Acta (BBA) - Protein Structure
Volume 236, Issue 1, 27 April 1971, Pages 211-221
Interaction of hemoglobin with ions: Allosteric effects of the binding of anions
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Cited by (23)
Early years of cytochrome P450 research in Berlin-Buch: Its present state and origin of the biochemical and biophysical conferences
2003, Biochemical and Biophysical Research CommunicationsCitation Excerpt :By their results the question of the influence of the protein moiety on the oxygen binding function of hemoglobin obtained a molecular basis. Therefore the studies on methemoglobin were complemented by physiologically relevant studies on the binding behaviour of oxygen and alkylisocyanides (as models for oxygen) in dependence on allosteric effectors such as organic (ATP, ADP) and inorganic (for instance, inositolhexa (-penta) phosphates [9,10]. These investigations also included questions of the stability of the protein and the relationship between the amino acid composition and the binding behaviour of hemoglobin.
Interaction of hemoglobin with salts. Effects on the functional properties of human hemoglobin
1981, Journal of Molecular Biology369 - Permanent multiplication of oxygen transport into tissues by combining the oxygen multistep therapy with lowering the oxygen binding capacity in the blood
1980, Bioelectrochemistry and BioenergeticsPermanent multiplication of oxygen transport into tissues by combining the oxygen multistep therapy with lowering the oxygen binding capacity in the blood
1980, Journal of Electroanalytical ChemistryThe conversion of trivalent to divalent iron in hemoglobin of various species
1975, Analytical Biochemistry
Copyright © 1971 Published by Elsevier B.V.