Results 141 to 150 of about 325,201 (172)
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The Journal of Nutritional Biochemistry, 2001
The objective of this study was to examine the in vitro hydrolysis of vitamin E esters (alpha-tocopheryl acetate, alpha-tocopheryl succinate and alpha-tocopheryl nicotinate) by pancreatic carboxyl ester hydrolase (CEH) at the concurrent presence of different bile acids at different concentrations.
C, Lauridsen +2 more
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The objective of this study was to examine the in vitro hydrolysis of vitamin E esters (alpha-tocopheryl acetate, alpha-tocopheryl succinate and alpha-tocopheryl nicotinate) by pancreatic carboxyl ester hydrolase (CEH) at the concurrent presence of different bile acids at different concentrations.
C, Lauridsen +2 more
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Carboxylic Ester Hydrolase and Amylase in Ischemic Pancreatitis in the Guinea Pig
Pancreas, 1996The observation that an elevated level of pancreatic carboxylic ester hydrolase (CEH) in serum is a more sensitive and specific marker of acute pancreatitis than is elevated serum amylase activity prompted us to explore whether these findings could be confirmed in an experimental model and, if so, to find the explanation behind this difference.
P J, Blind +4 more
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Binding of human pancreatic carboxylic ester hydrolase to lipid interfaces
Biochimica et Biophysica Acta (BBA) - Enzymology, 1981Human pancreatic carboxylic ester hydrolase (EC 3.1.1.1), usually characterized by its activity on water-soluble substrates, is shown to catalyze reactions taking place at a lipid/water interface. The inhibition of tributyrin hydrolysis by 1-alcohols follows the pattern of a Langmuir adsorption isotherm.
D, Lombardo, O, Guy
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Specific assay of carboxyl ester hydrolase using PEG esters as substrate
Analytical Methods, 2010The bile salt-stimulated lipase or carboxyl ester hydrolase (CEH) is a non-specific enzyme secreted by the exocrine pancreas and mammary glands. Recently we demonstrated that PEG esters were good substrates for CEH as it exhibited the highest specific activity ever recorded for this enzyme on PEG-8 monocaprylate.
Sylvie Fernandez +7 more
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A modified assay procedure for carboxylic ester hydrolases
Clinica Chimica Acta, 1969Abstract 1-Naphthol (α-naphthol) released by enzymatic hydrolysis from 1-naphthylacetate and other carboxylic esters can be determined by a condensation reaction with 4-amino-antipyrine and K3Fe(CN)6 in alkaline incubation mixtures. The condensation product has a red color which is soluble in ethyl acetate and other organic solvents.
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Structure–function relationships in the carboxylic‐ester‐hydrolase superfamily
European Journal of Biochemistry, 2000CNBr fragments from porcine intestinal glycerol‐ester hydrolase were separated by SDS/PAGE under reducing and nonreducing conditions, and their amino‐acid sequences were analysed. Two intra‐chain disulfide bridges were identified, namely Cys70–Cys99 (loop A) and Cys256–Cys267 (loop B).
S, Smialowski-Fléter +3 more
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Carboxylic Ester Hydrolase Activity in Hairless and Athymic Nude Mouse Skin
Pharmaceutical Research, 1990The carboxylic ester hydrolase activity was compared in athymic nude mouse skin and hairless mouse skin with respect to hydrolytic ability, heat inactivation, pH optima, and substrate specificity. Five aliphatic 5'-esters of 5-iodo-2'-deoxyuridine (IDU) were incubated with skin homogenate preparations, and the effect of linear chain length and ...
M K, Ghosh, A K, Mitra
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Effect of alcohols on the hydrolysis catalyzed by human pancreatic carboxylic-ester hydrolase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1981Transfer reactions catalyzed by human pancreatic carboxylic-ester hydrolase (EC 3.1.1.1) were studied in the presence of methanol and butanol as nucleophiles. The addition of alcohols produced an increase in the total rate of 4-nitrophenyl acetate and n-propylthiol acetate disappearance and a concomitant slow decrease of the hydrolysis rate.
D, Lombardo, O, Guy
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Immunocytochemical localization of pancreatic carboxylic ester hydrolase in human paneth cells
Histochemistry, 1986The protein-A gold method using specific rabbit sera directed against pure human pancreatic chymotrypsinogen and carboxylic ester hydrolase was applied to locate these (pro)enzymes in human pancreatic acinar cells and intestinal Paneth cells. Quantitative evaluation of the labelling indicated that both (pro)enzymes are present in pancreatic acinar ...
P, Lechene de la Porte +2 more
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Catalytic properties of modified human pancreatic carboxylic-ester hydrolase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Human pancreatic carboxylic-ester hydrolase (EC 3.1.1.1) modified by specific reagents (diisopropyl phosphorofluoridate, diethyl p-nitrophenyl phosphate, Woodward's K reagent and ethoxyformic anhydride) was studied for its activity. The three residues probably implicated in the active site acting on soluble substrate are shown to be essential for the ...
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