Results 151 to 160 of about 325,201 (172)

Purification and characterization of a carboxyl ester hydrolase from human pancreatic juice

Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
A carboxyl ester hydrolase has been purified 20-fold from human pancreatic juice. It is a glycoprotein with a molecular weight of 100 000. It contains 9% neutral and amino carbohydrates and the amino acid composition is characterized by a high content of proline residue (12.7%).
D, Lombardo, O, Guy, C, Figarella
openaire   +2 more sources

Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Purified carboxyl ester hydrolase (carboxylic-ester hydrolase, EC 3.1.1.1) from human pancreatic juice was found to hydrolyze triacetin, methyl butyrate and glycerides solubilized by bile salts. It has no activity on substrate presented as emulsoin or monomolecular films.
D, Lombardo, J, Fauvel, O, Guy
openaire   +2 more sources

Esterification of cholesterol and lipid-soluble vitamins by human pancreatic carboxyl ester hydrolase

Biochimie, 1980
Human pancreatic carboxyl ester hydrolase is shown to catalyse the esterification of cholesterol and lipid-soluble vitamins A, E and D3 with oleic acid. The acitivity requires the presence of bile salts, and the trihydroxylated or the 3 alpha, 7 alpha dihydroxylated bile salts are better activators than the 3 alpha, 12 alpha dihydroxylated bile salts ...
D, Lombardo, P, Deprez, O, Guy
openaire   +2 more sources

Molecular weight estimation of two carboxylic ester hydrolases ofEscherichia coli

Experientia, 1975
Des electrophoreses a diverses concentrations d'acrylamide montrent que les carboxyliques esters hydrolases A et B d'E. coli possedent des poids moleculaires distincts: 52,000 et 63,000 daltons. Les variations de mobilite observees selon les souches proviennent essentiellement de differences dans les charges electriques.
openaire   +2 more sources

Modification of the essential amino acids of human pancreatic carboxylic-ester hydrolase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
Chemical modification of human pancreatic carboxylic-ester hydrolase (EC 3.1.1.1) were performed using organophosphorus compounds, ethoxyformic anhydride and Woodward's K reagent. It has been shown that: (1) the inhibition of the enzyme activity by organophosphorus compounds is due to the phosphorylation of only one alcohol residue, probably a serine ...
openaire   +2 more sources

Hydrolysis of fluorescent pyrene‐acyl esters by human pancreatic carboxylic ester hydrolase and bile salt‐stimulated lipase

Lipids, 1990
AbstractFluorescent esters containing pyrenedecanoic acid (P10) or pyrenebutanoic (P4) acid (P4cholesterol, P10cholesterol, P4‐ and P10‐containing triacylglycerols) were synthesized and used as substrates for human pancreatic carboxylic ester hydrolase and bile salt‐stimulated lipase from human milk.
A, Negre-Salvayre, N, Abouakil, D, Lombardo, R, Salvayre   +3 more
openaire   +2 more sources

Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase

Biochemistry, 1986
A new substrate for ubiquitin carboxyl-terminal hydrolase, the carboxyl-terminal ethyl ester of ubiquitin, has been synthesized by a trypsin-catalyzed transpeptidation. In the presence of 1.6 M glycylglycine ethyl ester, trypsin removes the carboxyl-terminal glycylglycine of ubiquitin and replaces it with the dipeptide ester.
K D, Wilkinson, M J, Cox, A N, Mayer, T, Frey   +3 more
openaire   +2 more sources

Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Evidence is presented that human carboxyl ester hydrolase (carboxylic-ester hydrolase, EC 3.1.1.1) is able to hydrolyze cholesterol esters and lipid-soluble vitamins A, D-3 and E esters. Those activities require the presence of bile salts and the 3 alpha, 7 alpha-dihydroxylated bile salts have been found the most efficient activators.
D, Lombardo, O, Guy
openaire   +2 more sources

p-Nitrophenylacetate as a Substrate for a Carboxyl-ester Hydrolase in Pancreatic Juice and Intestinal Content

Scandinavian Journal of Gastroenterology, 1970
Erlanson, Charlotte 1970. p-Nitrophenylacetate as a Substrate for a Carboxylester Hydrolase in Pancreatic Juice and Intestinal Content. Scand. J. Gastroent.
openaire   +2 more sources

Carboxylic ester hydrolases in the thyroid gland of the guinea-pig. A light microscopic study

The Histochemical Journal, 1976
The location of cholinesterase and non-specific esterase in the thyroid gland of the guniea-pig was studied with the light microscope. It was found that the idoxyl method for non-specific esterase activity under special conditions is superior to the cholinesterase method in a number of respects for the demonstration of the intra-, inter- and ...
openaire   +3 more sources