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. 1984 Oct 1;223(1):61-6.
doi: 10.1042/bj2230061.

Purification and photoaffinity labelling of lipid methyltransferase from rat liver

M A Pajares, S Alemany, I Varela, D Marin Cao, J M Mato

Purification and photoaffinity labelling of lipid methyltransferase from rat liver

M A Pajares et al. Biochem J. .

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.

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