The effect of ligand on the kinetics of the sulfhydryl groups of human hemoglobin with p-mercuribenzoate.
The rate of reaction of PMB with the masked sulfhydryls of human hemoglobin derivatives correlates well with the extent of dissociation for various ligands. It is suggested that the alpha1beta2 dimer of hemoglobin participates in the slow step of the reaction with PMB.
D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008626:Mercuribenzoates; D008706:Methemoglobin / Q000031:analogs & derivatives; D013438:Sulfhydryl Compounds
D006454:Hemoglobins; D008024:Ligands; D008626:Mercuribenzoates; D013438:Sulfhydryl Compounds; D008706:Methemoglobin