[Modification of the alpha-subunit of phenylalanyl-tRNA synthetase from E. coli MRE-600 with N-chlorambucilyl-phenylalanyl-tRNA].
L-Phenylalanyl-tRNA synthetase from E. coli MRE-600 (EC 6.1.1.20) was alkylated with N-chlorambucilyl-[14C] phenylalanyl-tRNA. After removal of the affinity reagent tRNA moiety bp alkaline hydrolysis of the ester bond between the N-chlorambucilyl-phenylalanyl residue and the 3'-end of tRNA, The enzyme was dissociated into subunits in the presence of SDS. Separation of the subunits was performed by SDS electrophoresis. The bulk of the radioactivity of the N-chlorambucilyl-[14C] phenylalanyl residue was found at the position of the alpha-subunit of the enzyme. The results obtained are consistent with a specific binding of the phenylalanyl-tRNA analog to the alpha-subunit of the enzyme followed by covalent binding of the N-chlorambucilyl-phenylalanyl moiety to the protein.
D000345:Affinity Labels; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D002699:Chlorambucil; D004926:Escherichia coli / Q000201:enzymology*; D010649:Phenylalanine; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D011485:Protein Binding; D012343:RNA, Transfer
D000345:Affinity Labels; D002699:Chlorambucil; D010649:Phenylalanine; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase
Modifikatsiia al'fa- subdedinitsy fenilalanil-tRNK sintetazy iz E. coli MRE-600 s pomoshch'iu N-khlorambutsilili-fenilalanl-tRNK.