Esterolytic activities of rat intestinal mucosa. 2. Purification and properties of a glycerol-ester hydrolase.
A glycerol-ester hydrolase from rat intestinal cells has been purified using chromatography on carboxyhexanoyl-Sepharose-glyceryldioctanoate and preparative gel electrophoresis. The enzyme gives a single band by analytical gel electrophoresis; it is a monomer of molecular weight 68000. The optimum pH for its action on glyceryl tributyrate is between 8.0 and 8.5; the activation energy was calculated to be 8.7 kcal x mol-1 (36.4 kJ/mol). Its substrate specificity is mainly directed against esters of glycerol and of primary monoalcohols. Similarly to pancreatic lipase but contrary to liver esterase, it is inhibited by bile salts; relief of this inhibition by colipase is only observed for pancreatic lipase. The possible role of the glycerol-ester hydrolase in the absorption of short and of medium chain triglycerides is discussed.
D000818:Animals; D001647:Bile Acids and Salts / Q000494:pharmacology; D004075:Diglycerides; D004355:Drug Stability; D005989:Glycerides; D006863:Hydrogen-Ion Concentration; D007413:Intestinal Mucosa / Q000201:enzymology*; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D008297:Male; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D011092:Polyethylene Glycols; D051381:Rats; D013329:Structure-Activity Relationship; D013552:Swine; D013696:Temperature; D014280:Triglycerides
D001647:Bile Acids and Salts; D004075:Diglycerides; D005989:Glycerides; D014280:Triglycerides; D011092:Polyethylene Glycols; D008049:Lipase