title: Study of kinetics of thermal aggregation of mitochondrial aspartate aminotransferase by dynamic light scattering: protective effect of alpha-crystallin.
abstract: Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been studied at various temperatures and various protein concentrations by dynamic light scattering. The character of the dependence of protein aggregate size on time indicates that aggregation of mAAT proceeds in the regime of diffusion-limited cluster-cluster aggregation. Suppression of mAAT aggregation by alpha-crystallin is due to transition of the aggregation process into the regime of reaction-limited cluster-cluster aggregation. Realization of this regime of aggregation means that the sticking probability for the colliding particles is less than unity.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
authors.forename: Nikolay V
authors.initials: NV
authors.lastname: Golub
authors.forename: Kira A
authors.initials: KA
authors.lastname: Markossian
authors.forename: Mikhail V
authors.initials: MV
authors.lastname: Sholukh
authors.forename: Konstantin O
authors.initials: KO
authors.lastname: Muranov
authors.forename: Boris I
authors.initials: BI
authors.lastname: Kurganov
mesh_terms: D000818:Animals; D024442:Aspartate Aminotransferase, Mitochondrial / Q000737:chemistry* / Q000378:metabolism*; D002417:Cattle; D007700:Kinetics; D008027:Light; D011485:Protein Binding / Q000187:drug effects; D012542:Scattering, Radiation; D013696:Temperature; D038201:alpha-Crystallins / Q000494:pharmacology*
chemical_list: D038201:alpha-Crystallins; D024442:Aspartate Aminotransferase, Mitochondrial