Autor: |
Verkhogliad IN, Vinogradova RP, Kucherenko NE |
Jazyk: |
ruština |
Zdroj: |
Ukrainskii biokhimicheskii zhurnal (1978) [Ukr Biokhim Zh (1978)] 1985 Jul-Aug; Vol. 57 (4), pp. 19-23. |
Abstrakt: |
Two lysyl-tRNA-synthetase forms are obtained from the rat liver. Their molecular masses are determined by electrophoresis and gel-filtration on Sephadex G-150: form I-122, form II-64 kDalton. Gel-electrophoresis in the presence of 0.1% SDS indicates that form I of lysyl-tRNA-synthetase consists of two subunits with a molecular mass of 64 kDalton each, i. e. it is a dimer. Optimal conditions and kinetic parameters (Km and Vmax) of aminoacylation for the both enzyme forms are similar. Amino acid composition, fluorescence parameters and thermal inactivation conditions are determined. |
Databáze: |
MEDLINE |
Externí odkaz: |
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