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Biochemical Pharmacology, 1974 Some of the next articles are maybe not open access.
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Purification and characterization of a carboxyl ester hydrolase from human pancreatic juice
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978A 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
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Current Protocols in Toxicology, 2002
AbstractAssays for the Classification of Two Types of Esterases: Carboxylic Ester Hydrolase and Phosphoric Triester Hydrolase (Douglas D. Anspaugh and Michael Roe, North Carolina State University, Raleigh, North Carolina). This unit describes assays that quantitate two types of esterase the carboxylic ester hydrolases and the phosphoric triester ...
Douglas D, Anspaugh, R Michael, Roe
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AbstractAssays for the Classification of Two Types of Esterases: Carboxylic Ester Hydrolase and Phosphoric Triester Hydrolase (Douglas D. Anspaugh and Michael Roe, North Carolina State University, Raleigh, North Carolina). This unit describes assays that quantitate two types of esterase the carboxylic ester hydrolases and the phosphoric triester ...
Douglas D, Anspaugh, R Michael, Roe
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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
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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
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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
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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
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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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Carboxyl ester hydrolases production and growth of a halophilic archaeon, Halobacterium sp. NRC-1
Extremophiles, 2009The capability of Halobacterium sp. NRC-1 to synthesize carboxyl ester hydrolases was investigated, and the effect of physicochemical conditions on the growth rate and production of esterases was evaluated. The haloarchaeon synthesized a carboxyl ester hydrolase, confirming the genomic prediction. This enzymatic activity was intracellularly produced as
Rosa María, Camacho +4 more
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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 +3 more
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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 +3 more
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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
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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
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Carboxylic ester hydrolases in the thyroid gland of the guinea-pig. A light microscopic study
The Histochemical Journal, 1976The 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 ...
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