[Monoclonal antibodies against tryptophanyl-tRNA-synthetase].
Monoclonal antibodies designated as Am1 and Am2 were prepared against purified beef pancreas tryptophanyl-tRNA synthetase (EC 6.1.1.2). Both antibodies were able to bind the native enzyme in a solid-phase assay and to precipitate enzyme activity in immune complexes. Am2 inhibited the tryptophanyl-tRNA synthetase activity in ATP-[32P]pyrophosphate exchange and in tRNATrp aminoacylation reactions; Am1 had no influence on both the enzyme activity and the inhibiting action of Am2. Only Am2, not Am1, bound elastase-modified form of the enzyme which consists of two subunits shortened by 20 000 daltons from the N-end of the molecule. These results were interpreted as an evidence for non-overlapping of Am1 and Am2 antigenic determinants along the polypeptide chains of the enzyme.
D000604:Amino Acyl-tRNA Synthetases / Q000276:immunology*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D002417:Cattle; D006825:Hybridomas; D051379:Mice; D008807:Mice, Inbred BALB C; D010179:Pancreas / Q000201:enzymology; D011863:Radioimmunoassay; D051381:Rats; D014369:Tryptophan-tRNA Ligase / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase
Monoklonal'nye antitela k triptofanil-tRNK-sintetaze.