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• W1995556020 abstract "Various parameters which affect the binding of aquocobalamin (aquo-B12) to bovine serum albumin (BSA) were examined. Binding at pH 7.4 was markedly dependent on the time of incubation, the temperature and the concentration of aquo-B12. Aquo-B12 was bound to both the monomer and the dimer fractions in the BSA preparation and was not influenced by p-chloromercuribenzoate titration of the SH group. Approximately 70% of the bound aquo-B12 dissociated at pH 4.0 and all of it was readily removed with KCN. The tight binding of aquo-B12 at pH 7.4 was independent of the phosphate buffer concentration but was increased 2-fold in the presence of 5 m urea. Among seven other corrinoid compounds which were tested only diaquocobinamide formed a stable complex with BSA. Isolated complexes containing 0.6–2.6 moles of B12/mole of BSA were red-violet in color. They closely mimicked the complex formed between aquo-B12 and imidazole (or 1-methyl imidazole) in their absorption and their circular dichroism spectra. In addition, the pH curve for the binding of aquo-B12 to BSA was like that for the formation of an aquo-B12-imidazole complex. Equilibrium dialysis indicated that the maximum number of BSA combining sites was 16. From the above findings it was concluded that the binding reaction of aquo-B12 to BSA occurs between the sixth coordinating position of the cobalt and the imidazole side chains." @default.
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• W1995556020 date "1970-11-01" @default.
• W1995556020 modified "2023-09-26" @default.
• W1995556020 title "Binding of aquocobalamin to the histidine residues in bovine serum albumin" @default.
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• W1995556020 doi "https://doi.org/10.1016/0003-9861(70)90129-3" @default.
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