Mechanism of chaperone-like activity. Suppression of thermal aggregation of betaL-crystallin by alpha-crystallin.

Abstract

Thermal denaturation and aggregation of beta(L)-crystallin from bovine lens have been studied using differential scanning calorimetry (DSC) and dynamic light scattering (DLS). According to the DLS data, the distribution of the beta(L)-crystallin aggregates by their hydrodynamic radius (R(h)) remains monomodal to the point of precipitating aggregates (sodium… (More)

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@article{Khanova2005MechanismOC, title={Mechanism of chaperone-like activity. Suppression of thermal aggregation of betaL-crystallin by alpha-crystallin.}, author={Helen A Khanova and Kira A. Markossian and Boris I. Kurganov and Alexander M Samoilov and Sergey Yu Kleimenov and Dmitrii I Levitsky and Igor K. Yudin and Antonina C Timofeeva and Konstantin Muranov and Michail A Ostrovsky}, journal={Biochemistry}, year={2005}, volume={44 47}, pages={15480-7} }