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Chemical modification of the tryptophan residues of leucyl-tRNA synthetase by N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide

Journal Article · · Sov. J. Bioorg. Chem. (Engl. Transl.); (United States)
OSTI ID:5347529
The accessibility for modification of the tryptophan residues in leucyl-tRNA synthetase from cow mammary glands has been studied with the aid of the specific chemical reagents N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide. UV absorption and the intrinsic fluorescence of the tryptophan residues of the enzymes were used for recording the course of the modification. It has been shown that under native conditions (pH 7.8) two superficial residues in each subunit of the dimeric enzyme undergo modification. Under denaturing conditions (6 M guanidine hydrochloride), the internal tryptophan residues are also modified. When the tryptophan residues are modified, the leucyl-tRNA synthetase is inactivated both in the aminoacylation reaction and in the ATP-PP/sub i/ exchange reaction. In the specific complex of leucyl-tRNA synthetase with tRNA/sup Leu/ one of the superficial tryptophan residues is screened and does not undergo modification by the reagents used
Research Organization:
Institute of Molecular Biology and Genetics, Kiev (USSR)
OSTI ID:
5347529
Journal Information:
Sov. J. Bioorg. Chem. (Engl. Transl.); (United States), Journal Name: Sov. J. Bioorg. Chem. (Engl. Transl.); (United States) Vol. 11:5; ISSN SJBCD
Country of Publication:
United States
Language:
English

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