Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells

Can J Biochem Cell Biol. 1985 May;63(5):341-7. doi: 10.1139/o85-050.


We have purified the monoacylglycerol acyltransferase from rat small intestinal mucosa to homogeneity by a combination of hydrophobic absorption, guanidine dissociation, and gel filtration. The purified enzyme gives a single band of 37 000 daltons on sodium dodecyl sulphate--polyacrylamide gel electrophoresis. The enzyme has a specific activity of about 5900 nmol/mg per hour and represents 0.12% of total cell protein, corresponding to about a 600-fold purification. The enzyme does not acylate diacylglycerols to triacylglycerols, which is consistent with the separate physical existence of the mono- and di-acylglycerol acyltransferases. The enzyme acylates the 2-monoacylglycerols to yield an essentially racemic mixture of diacylglycerols. It does not acylate glycerol-3-phosphate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / antagonists & inhibitors
  • Acyltransferases / isolation & purification*
  • Amino Acids / analysis
  • Animals
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Hydrogen-Ion Concentration
  • Intestinal Mucosa / enzymology*
  • Intestinal Mucosa / ultrastructure
  • Intestine, Small / enzymology
  • Male
  • Microsomes / enzymology
  • Molecular Weight
  • Rats
  • Rats, Inbred Strains
  • Sodium Dodecyl Sulfate
  • Stereoisomerism


  • Amino Acids
  • Sodium Dodecyl Sulfate
  • Acyltransferases
  • 2-acylglycerol O-acyltransferase