On the Mechanisms of pH-dependent Hydrogen Exchange of Bovine Plasma Albumin in the Range of pH 5 to 8.5

摘要: Hydrogen exchange rates of bovine plasma albumin vary over the range pH 5 to 8.5. As is raised, number very slowly exchanging hydrogens decreases and rapidly steadily increases. The rate core at was studied values from 5.2 results obtained suggest that this protein highly "motile"; is, it fluctuates 7 above between states in which exchangeable are accessible bulk solvent ones they not accessible. In 6.5, no segments appear be motile but compact may become as raised through range. alternative possibility, changes behavior 6.5 local environment individual groups, cannot excluded. effects sodium dodecyl sulfate, glycerol, changing ionic strength were also 7.7. consistent with three possible explanations: (a) these agents stabilize conformational albumin; (b) reduce segmental "motility;"; or (c) alter groups thus influence dependencies units. Discrimination mechanisms deemed on basis our experimental data.