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Nucleic Acids Research, 1977, Vol. 4, No. 7 2123-2136
© 1977

Articles

The characterization of phosphoseryl tRNA from lactating bovine mammary gland

Stephen J. Sharp and Thomas S. Stewart

School of Biochemistry, University of New South Wales P. O. Box 1, Kensington, N.S.W. 2033, Australia

Received February 3, 1977. BD-cellulose and RPC-5 chromatography of tRNA iso lated from lactating bovine mammary gland showed the presence of four seryl-tRNA isoacceptors. The species, tRNAFormula with the strongest affinity for BD-cellulose (required ethanol in the elution buffer) could be phosphorylated in the presence of serine, [{gamma}-32P]-ATP, seryl-tRNA synthetase and phosphotransferase activity from the same tissue. O-Phosphoserine was identified as the 32P-labbled 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.


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