Immuno-chemical non-cross-reactivity between eukaryotic and prokaryotic seryl-tRNA synthetases

Monospecific polyclonal antibodies (pAbs) against highly purified bovine seryl-tRNA synthetase (SerRS, EC 6.1.1.1) were prepared and their specificity tested. The interactions of pAbs with SerRS from different organisms were investigated by protein immunoblotting and ELISA methods. pAbs inhibit euka...

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Veröffentlicht in:	FEBS letters 1991-11, Vol.292 (1), p.76-78
Hauptverfasser:	Sidorik, L.L., Gudzera, O.I., Dragovoz, V.A., Tukalo, M.A., Beresten, S.F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Antibodies Biological and medical sciences Blotting, Western bovine serum albumin BSA Cattle Cross Reactions E coli Enzyme-Linked Immunosorbent Assay Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Immunochemical cross-reaction Immunohistochemistry Ligases Liver - enzymology Monospecific polyclonal antibody pAbs PBS phenylmethylsulphonyl fluoride PMSF rabbit monospecific polyclonal antibodies against bovine SerRS Rabbits SDS Serine-tRNA Ligase - immunology Serine-tRNA Ligase - metabolism SerRS Seryl-tRNA synthetase sodium dodecylsulphate sodium phosphate buffer
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Zusammenfassung:	Monospecific polyclonal antibodies (pAbs) against highly purified bovine seryl-tRNA synthetase (SerRS, EC 6.1.1.1) were prepared and their specificity tested. The interactions of pAbs with SerRS from different organisms were investigated by protein immunoblotting and ELISA methods. pAbs inhibit eukaryotic SerRS aminoacylating activity and exert no effect on SerRS activity from prokaryotes. It is proposed that prokaryotic and eukaryotic SerRS evolve from different ancestor genes.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)80838-T