A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives.

ABSTRACT: Chemical chaperones including arginine and its derivatives are widely used by biochemists working on the design of agents, which are able to efficiently suppress protein aggregation. To elucidate the mechanisms of anti-aggregation activity of chemical chaperones, methods based on registration of the increment in light scattering intensity must be supplemented with methods for direct detection of the portion of aggregated protein (γ_agg). For this purpose asymmetric flow field-flow fractionation was used in the present work. It was shown that heat-induced aggregation of bovine serum albumin (BSA) followed the kinetics of the reaction of the second order (0.1 M sodium phosphate buffer, pH 7.0, 70 °C). It was proposed to use R _h vs γ_agg plots to characterize th

SUBMITTER: Borzova VA 

PROVIDER: S-EPMC5479853 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature