Glycerol-ester hydrolase from human small intestine and its possible role in the degradation of neutral lipids.
A glycerol-ester hydrolase has been characterized and partially purified (23-fold) from human small intestine. A pancreatic origin was excluded through the use of an immunoserum directed against human pancreatic juice, while a pharyngeal (gastric) origin was unlikely owing to the optimum pH range of activity of the gastric enzyme as compared to that of the intestinal enzyme. The glycerol-ester hydrolase is mainly active toward short- and medium-chain di- and triglycerides and toward micellar long-chain monoglycerides. A role in the absorption of neutral lipids, mainly in pathological situations, is postulated.
D001647:Bile Acids and Salts / Q000502:physiology; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007408:Intestinal Absorption; D007413:Intestinal Mucosa / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology*; D050356:Lipid Metabolism; D008286:Malabsorption Syndromes / Q000378:metabolism; D008994:Monoacylglycerol Lipases / Q000302:isolation & purification / Q000378:metabolism*; D013869:Thiolester Hydrolases / Q000302:isolation & purification
D001647:Bile Acids and Salts; D002265:Carboxylic Ester Hydrolases; D008994:Monoacylglycerol Lipases; D013869:Thiolester Hydrolases