Open AccessEsterolytic Activities of Rat Intestinal Mucosa
Author(s) -
FERNANDEZLOPEZ Victor,
SERRERO Ginette,
NÉGREL Raymond,
AILHAUD Gérard
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb11112.x
Subject(s) - colipase , chemistry , glycerol , lipase , esterase , biochemistry , chromatography , hydrolase , monomer , substrate (aquarium) , enzyme , pancreatic lipase , electrophoresis , organic chemistry , biology , ecology , polymer
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 × 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.