Esterolytic activities of rat intestinal mucosa. 1. Characterization, cellular distribution and subcellular localization of a glycerol-ester hydrolase.
The preferential cellular distribution in the villus tip and the subcellular localization in the endoplasmic reticulum of an intestinal glycerol-ester hydrolase from rat mucosa are described. The enzyme is shown not to be from either pancreatic or bacterial origin; it catalyzes the hydrolysis of short- and medium chain triglycerides and of p-nitrophenylacetate. Contrarily to the specificity found for the pig intestinal lipase (Serrero, Négrel and Ailhaud, 1975), no activity is detectable against acylCoA; a thiolester hydrolase different from the glycerol-ester hydrolase was demonstrated after differential solubilization and chromatographic separation. A high proportion of glycerol-ester hydrolase is present in the intestinal lumen; its possible complementary role in lipid degradation is discussed.
D000375:Aging; D000818:Animals; D005989:Glycerides; D006863:Hydrogen-Ion Concentration; D007413:Intestinal Mucosa / Q000201:enzymology* / Q000254:growth & development; D008049:Lipase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D011092:Polyethylene Glycols; D011233:Precipitin Tests; D051381:Rats; D012995:Solubility; D013347:Subcellular Fractions / Q000201:enzymology; D013501:Surface-Active Agents
D005989:Glycerides; D013501:Surface-Active Agents; D011092:Polyethylene Glycols; D008049:Lipase