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Vasopressin‐stimulated phosphorylation of rat liver phospholipid methyltransferase in isolated hepatocytes
Author(s) -
Mérida Isabel,
Varela Isabel,
Alvarez José F.,
Cabrero Carmen,
Mato José M.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80262-9
Subject(s) - phosphoserine , phospholipid , polyacrylamide gel electrophoresis , biochemistry , phosphorylation , gel electrophoresis , vasopressin , methyltransferase , chemistry , biology , immunoprecipitation , microbiology and biotechnology , enzyme , serine , endocrinology , membrane , dna , methylation , gene
Addition of vasopressin (1μM) to isolated rat hepatocytes prelabeled with [ 32 P]phosphate was accompanied by a 250% increase in the phosphorylation of phospholipid methyltransferase. Vasopressin‐stimulated phospholipid methyltransferase phosphorylation was time‐ and dose‐dependent. 32 P‐labeled phospholipid methyltransferase was recovered by immunoprecipitation and SDS‐polyacrylamide gel electrophoresis. After electrophoresis, phospholipid methyltransferase was electroeluted from the polyacrylamide gel and subjected to tryptic digestion or HCl hydrolysis. Analysis of 32 P‐labeled peptides reveals only one site of phosphorylation and the analysis of [ 32 P]phosphoamino acids indicates that phosphoserine is the only labeled amino acid.