Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells.
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.
D000217:Acyltransferases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007413:Intestinal Mucosa / Q000201:enzymology* / Q000648:ultrastructure; D007421:Intestine, Small / Q000201:enzymology; D008297:Male; D008861:Microsomes / Q000201:enzymology; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D012967:Sodium Dodecyl Sulfate; D013237:Stereoisomerism
D000596:Amino Acids; D012967:Sodium Dodecyl Sulfate; D000217:Acyltransferases; C021802:2-acylglycerol O-acyltransferase