[Study of hemoglobin structure using the allosteric label method].
The rate of human hemoglobin oxidation in the presence of various sulfhydryl reagents essentially depends on the degree of binding of different sulfhydryl groups of hemoglobin during the oxidation process. Kinetics of modified hemoglobin oxidation is biphasic, which allows to judge the effect of reagent-hemoglobin binding on the state of rapidly and slowly oxidated subunits separately.
D000494:Allosteric Regulation; D002263:Carboxyhemoglobin / Q000032:analysis / Q000378:metabolism; D006454:Hemoglobins / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D010084:Oxidation-Reduction; D010108:Oxyhemoglobins / Q000032:analysis / Q000378:metabolism; D011487:Protein Conformation; D013113:Spin Labels; D013439:Sulfhydryl Reagents / Q000378:metabolism
D006454:Hemoglobins; D010108:Oxyhemoglobins; D013113:Spin Labels; D013439:Sulfhydryl Reagents; D002263:Carboxyhemoglobin
Izuchenie struktury gemoglobina metodom 'allostericheskikh metok".