Characterization of the tryptophanyl enzyme obtained during denaturation of an active tryptophanyl derivative of tryptophanyl transfer rna synthetase
Moroz, S.G.; Krauspe, R.; Kovaleva, G.K.; Favorova, O.O.
Bioorganicheskaya Khimiya 5(8): 1248-1253
ISSN/ISBN: 0360-4497 Accession: 004934110
Upon the 8 M urea denaturation of the tryptophanyl-derivative of the [bovine pancreas] tryptophanyl-tRNA synthetase, a slow transfer of the tryptophanyl residue from a carboxylic group of the protein molecule to some other group takes place will concomitant replacement of the acid-labile bond for acid-stable one. The obtained tryptophanyl-enzyme derivative reacts with NH2OH forming tryptophanyl-hydroxamate and is labile at alkaline pH and after performic acid oxidation. The chemical properties of the obtained derivative indicate that it is the SH-group which is mainly responsible for accepting the tryptophanyl residue in the course of denaturation. By means of diagonal electrophoresis, a cystein-containing tryptic peptide which comprised the bound tryptophanyl moiety is isolated and its amino acid composition is established.