Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase |
| |
Authors: | Kira A Markossian Nikolay V Golub Natalia A Chebotareva Regina A Asryants Irina N Naletova Vladimir I Muronetz Konstantin O Muranov Boris I Kurganov |
| |
Institution: | (1) Bach Institute of Biochemistry, Russian Academy of Sciences, 119071 Moscow, Russia;(2) Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia;(3) Faculty of Bioengineering and Bioinformatics, Moscow State University, 119992 Moscow, Russia;(4) Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia |
| |
Abstract: | Effects of α-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
(GAPDH) have been studied using dynamic light scattering and analytical ultracentrifugation. The analysis of the initial parts
of the dependences of the hydrodynamic radius of protein aggregates on time shows that in the presence of α-crystallin or
GroEL the kinetic regime of GAPDH aggregation is changed from the regime of diffusion-limited cluster–cluster aggregation
to the regime of reaction-limited cluster–cluster aggregation, wherein the sticking probability for the colliding particles
becomes lower the unity. In contrast to α-crystallin, GroEL does not interfere with formation of the start aggregates which
include denatured GAPDH molecules. On the basis of the analytical ultracentrifugation data the conclusion has been made that
the products of dissociation of GAPDH and α-crystallin or GroEL play an important role in the interactions of GAPDH and chaperones
at elevated temperatures. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|