The characterization of phosphoseryl tRNA from lactating bovine mammary gland.
Nucleic Acids Res, 1977/7;4(7):2123-36.
PMID: 242796
Impact factor: 19.16
Abstract
BD-cellulose and RPC-5 chromatography of tRNA isolated from lactating bovine mammary gland showed the presence of four seryl-tRNA isoacceptors. The species, tRNA IV Ser, with the strongest affinity for BD-cellulose (required ethanol in the elution buffer) could be phosphorylated in the presence of serine, [gamma-32 P]-ATP, seryl-tRNA synthetase and phosphotransferase activity from the same tissue. O-Phosphoserine was identified as the 32P-labelled product after mild alkaline hydrolysis of this aminoacylated tRNA. Pancreatic ribonuclease treatment of the aminoacylated tRNA yielded a labelled product which was identified as phosphoseryladenosine. These results indicated there is a specific phosphoseryl tRNA species in lactating bovine mammary gland. It appears that the formation of phosphoseryl-tRNA proceeds by enzymic phosphorylation of seryl-tRNA.
MeSH terms
Amino Acyl-tRNA Synthetases; Animals; Cattle; Chromatography, Ion Exchange; Female; Lactation; Mammary Glands, Animal; Organophosphorus Compounds; Phosphotransferases; Pregnancy; RNA, Transfer, Amino Acyl; Serine
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