Effect of alpha-crystallin on thermostability of mitochondrial aspartate aminotransferase.
Effect of alpha-crystallin on thermal inactivation, denaturation and aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been in the focus of this study. Acceleration of heat-induced inactivation of mAAT was demonstrated in the presence of alpha-crystallin. According to the data of differential scanning calorimetry, alpha-crystallin induces destabilization of the mAAT molecule. The size of protein aggregates formed at heating of mAAT at a constant rate (1 degree C/min) has been defined by dynamic light scattering. The obtained data show that aggregation of mAAT in the presence of alpha-crystallin proceeds in the regime of reaction-limited cluster-cluster aggregation.
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia.
Kira A
KA
Markossian
Nikolay V
NV
Golub
Sergey Yu
SY
Kleymenov
Konstantin O
KO
Muranov
Mikhail V
MV
Sholukh
Boris I
BI
Kurganov
D001219:Aspartate Aminotransferases / Q000737:chemistry* / Q000378:metabolism; D004058:Diffusion; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability / Q000187:drug effects; D008928:Mitochondria / Q000201:enzymology*; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D013696:Temperature; D038201:alpha-Crystallins / Q000494:pharmacology*
D038201:alpha-Crystallins; D001219:Aspartate Aminotransferases