title: Evidence for the formation of start aggregates as an initial stage of protein aggregation.
abstract: The kinetics of thermal aggregation of glycogen phosphorylase b and glyceraldehyde 3-phosphate dehydrogenase from rabbit skeletal muscles were studied using dynamic light scattering. Use of high concentrations of the enzymes (1-3 mg/ml) provided a simultaneous registration of the native enzyme forms and protein aggregates. It was shown that initially registered aggregates (start aggregates) were large-sized particles. The hydrodynamic radius of the start aggregates was about 100 nm. The intermediate states between the native enzyme forms and start aggregates were not detected. The initial increase in the light scattering intensity is connected with accumulation of the start aggregates, the size of the latter remaining unchanged. From a certain moment in time aggregates of higher order, formed as a result of sticking of the start aggregates, make a major contribution to the enhancement of the light scattering intensity.
authors: Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia.
authors: Nikolay
authors: N
authors: Golub
authors: Alexey
authors: A
authors: Meremyanin
authors: Kira
authors: K
authors: Markossian
authors: Tatyana
authors: T
authors: Eronina
authors: Natalia
authors: N
authors: Chebotareva
authors: Regina
authors: R
authors: Asryants
authors: Vladimir
authors: V
authors: Muronets
authors: Boris
authors: B
authors: Kurganov
mesh_terms: D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry*; D024982:Glycogen Phosphorylase, Muscle Form / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D011817:Rabbits; D013696:Temperature
chemical_list: D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D024982:Glycogen Phosphorylase, Muscle Form