title: Purification and photoaffinity labelling of lipid methyltransferase from rat liver.
abstract: An enzyme that catalyses the three-step methylation of phosphatidylethanolamine to phosphatidylcholine as well as the methylation of fatty acids and that uses S-adenosylmethionine as the methyl donor has been purified about 200-fold from rat liver. Irradiation of the purified enzyme with a short-wavelength u.v. light in the presence of [methyl-3H]8-azido-S-adenosylmethionine followed by electrophoresis results in the incorporation of radioactivity into a single protein band of about 25 kDa. It is concluded that a single catalytic subunit catalyses the conversion of phosphatidylethanolamine into phosphatidylcholine and fatty acid methylation.
mesh_terms: D000345:Affinity Labels; D000818:Animals; D001386:Azides; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008745:Methylation; D051381:Rats; D012436:S-Adenosylmethionine / Q000031:analogs & derivatives
chemical_list: D000345:Affinity Labels; D001386:Azides; D012436:S-Adenosylmethionine; C037207:8-azido-S-adenosylmethionine