Zobrazeno 1 - 10
of 29
pro vyhledávání: '"G K, Kovaleva"'
Publikováno v:
Siberian Medical Review. :102-105
Autor:
S M, Elizarov, M Iu, Zabazarnykh, A Kh, Musoliamov, G K, Kovaleva, Ts A, Egorov, L L, Kiselev
Publikováno v:
Molekuliarnaia biologiia. 31(2)
Autor:
S M, Elizarov, G K, Kovaleva
Publikováno v:
Molekuliarnaia biologiia. 24(6)
Incubation of tryptophanyl-tRNA synthetase from bovine pancrease with [gamma-32P]ATP of [gamma-32P]GTP and casein kinase II from rabbit liver leads to the incorporation of labeled phosphate into serine residues of synthetase polypeptide. The maximal
Publikováno v:
Biopolymers and Cell. 2:179-185
Publikováno v:
Molecular Biology Reports. 8:17-20
The covalent derivative of the tryptophanyl-tRNA synthetase obtained under the action of32PPi contains one mole of the covalently bound pyrophosphate (or 2 moles of orthophosphate) per mole of dimeric enzyme. Dephosphorylation with alkaline phosphata
Publikováno v:
Biopolymers and Cell. 2:12-19
Publikováno v:
Bioorganicheskaia khimiia. 15(10)
Method of isolation of the bovine pancreas tryptophanyl-tRNA synthetase is improved and a protein with greater than or equal to 99% purity, according to PAGE-SDS, is obtained. The pure enzyme is digested with clostripain and the hydrolysate is separa
Publikováno v:
Molekuliarnaia biologiia. 18(5)
The possibility of participation of covalent enzyme substrate's derivatives in reactions catalyzed by aminoacyl-tRNA synthetases is discussed in connection with general principles of enzyme catalysis. Tryptophanylated and pyrophosphorylated forms of
Publikováno v:
Molekuliarnaia biologiia. 12(3)
The catalytic groups, involved in aminoacyl-tRNA formation remain unknown. The isolation and identification of an active covalent complex between the enzyme and substrate is an essential step in understanding the reaction mechanism. We identified and
Publikováno v:
Molekuliarnaia biologiia. 15(1)
Kinetic parameters of the reaction of ATP-PPi exchange, catalysed by "one-site" form of beef pancreas tryptophanyl-tRNA-synthetase are determined. The one-site form was obtained by affinity labelling of one active centre of the enzyme with alkylated