Stereospecificity of monoacylglycerol acyltransferase activity from rat intestine and suckling rat liver.

Journal Article (Journal Article)

The stereospecificity of monoacylglycerol acyltransferase from rat intestinal mucosa and suckling rat liver microsomes was examined using sn-1,2-diacylglycerol kinase from Escherichia coli. With 2-monooleoyl glycerol and palmitoyl-CoA, 88 and 87.9% of the diacylglycerol synthesized by the intestinal mucosa and suckling liver, respectively, was demonstrated to be the sn-1,2-isomer. Analysis of similar preparations of these diacylglycerol products by gas-liquid chromatography-mass spectrometry indicated that most of the remaining diacylglycerol was the 1,3-isomer that probably arose via acyl-migration. These results indicate that monoacylglycerol acyltransferase is stereospecific. Measurement of acyltransferase activities in microsomes using 1- and 2-monoacyl- and monoalkylglycerols as substrates indicated that the monoacylglycerol acyltransferases from suckling liver and intestinal mucosa have different substrate specificities.

Full Text

Duke Authors

Cited Authors

  • Coleman, RA; Walsh, JP; Millington, DS; Maltby, DA

Published Date

  • February 1, 1986

Published In

Volume / Issue

  • 27 / 2

Start / End Page

  • 158 - 165

PubMed ID

  • 3958618

International Standard Serial Number (ISSN)

  • 0022-2275


  • eng

Conference Location

  • United States