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- W2053442664 abstract "The buoyant density of bovine serum mercaptalbumin was measured in CsCl throughout the pH range 5.0–12.5. The buoyant densities were found to increase gradually until a sharp increase was noted at pH 10.5. These data were analyzed in terms of changes in water and salt binding as the ionizable amino acid residues titrate. The recent data of Foster were used to compute the charge on the molecule as a function of pH. A generalized equation expressing the buoyant density was combined with the condition that the molecule be electrically neutral to yield the number of Cs+ and Cl− bound as a function of pH. The results indicate a generalized increase and decrease in the number of Cs+ and Cl−, respectively, bound as the pH is raised from the isoelectric pH of 5.3 to pH 9.5. As the pH continues to rise, a large increase in the number of Cs+ bound is noted as the tyrosines are ionized, and a sharp decrease in the number of Cl− bound as the lysine residues are deprotonated." @default.
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- W2053442664 date "1969-05-01" @default.
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- W2053442664 title "The buoyant titration of bovine serum mercaptalbumin I. An interpretation in terms of ion binding" @default.
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- W2053442664 doi "https://doi.org/10.1016/0005-2795(69)90254-2" @default.
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