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 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.
Sidorik
L L
LL
Institute of Molecular Biology and Genetics, Ukrainian Academy of Sciences, Kiev, USSR.
Gudzera
O I
OI
Dragovoz
V A
VA
Tukalo
M A
MA
Beresten
S F
SF
D000818:Animals; D000906:Antibodies; D015153:Blotting, Western; D002417:Cattle; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000201:enzymology; D007150:Immunohistochemistry; D008099:Liver / Q000201:enzymology; D011817:Rabbits; D012714:Serine-tRNA Ligase / Q000276:immunology / Q000378:metabolism*
D000906:Antibodies; D012714:Serine-tRNA Ligase