Results 151 to 160 of about 14,952 (193)
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Carboxylesterases (EC 3.1.1.). A large-scale purification of pig liver carboxylesterase
Biochemistry, 1969Two procedures for the large-scale purification of pig liver carboxylesterase are described. They start from chloroform-acetone powders of minced pig liver and involve ammonium sulfate fractionation, chromatography on CM-cellulose and CM-Sephadex, and gel filtration. These procedures produce an enzyme of hitherto unobtained purity.
Horgan, Douglas J. +3 more
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Structure, function and regulation of carboxylesterases
Chemico-Biological Interactions, 2006This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we have proposed a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. In addition, mechanisms of
Tetsuo, Satoh, Masakiyo, Hosokawa
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Molecular Cancer Therapeutics, 2004
Abstract Carboxylesterases, expressed at high levels in human liver and intestine, are thought to detoxify xenobiotics. The anticancer prodrug 7-ethyl-10-[4-1-piperidino)-1-piperidino]carbonyloxycamptothecin (CPT-11) is also metabolized by carboxylesterases to produce the active drug 7-ethyl-10-hydroxycamptothecin.
Kyoung Jin P, Yoon +5 more
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Abstract Carboxylesterases, expressed at high levels in human liver and intestine, are thought to detoxify xenobiotics. The anticancer prodrug 7-ethyl-10-[4-1-piperidino)-1-piperidino]carbonyloxycamptothecin (CPT-11) is also metabolized by carboxylesterases to produce the active drug 7-ethyl-10-hydroxycamptothecin.
Kyoung Jin P, Yoon +5 more
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Carboxylesterases (EC 3.1.1). The Molecular Sizes of Chicken and Pig Liver Carboxylesterases
Canadian Journal of Biochemistry, 1975The molecular size of pig liver carboxylesterase has been investigated under a variety of conditions of pH and ionic strength. From equilibrium and velocity sedimentation at pH 4.0 and pH 7.5, and from chromatography on Sephadex G-200, we conclude that the monomeric molecular weight is ~65 000 daltons and that the enzyme associates to form trimers ...
P A, Inkerman, D J, Winzor, B, Zerner
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KINETICS FOR THE INHIBITION OF CARBOXYLESTERASE BY MALAOXON
Canadian Journal of Biochemistry, 1967Malaoxon and carboxylesterase undergo two separate but simultaneous reactions when mixed in solution. One results in the irreversible inhibition of carboxylesterase. In the other, malaoxon acts as a substrate and is hydrolyzed.This work is concerned primarily with the inhibition reaction, although direct evidence of the substrate reaction is also given.
A R, Main, W C, Dauterman
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Thermostable Carboxylesterases from Hyperthermophiles
ChemInform, 2004AbstractFor Abstract see ChemInform Abstract in Full Text.
Atomi, H, Imanaka, T
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Enzymatic Activity of Human Carboxylesterases
Current Protocols in Toxicology, 2007AbstractThe carboxylesterases (CEs) are hydrolytic enzymes that metabolize xenobiotics that contain ester, thioester, or amide bonds. CEs are ubiquitously expressed but are found in highest concentration in membrane‐enriched fractions of the liver. This unit describes assays used to measure the enzymatic activity and tissue distribution of human CEs ...
Matthew K, Ross, Abdolsamad, Borazjani
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The carboxylesterases of Trypanosoma cruzi epimastigotes
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1987Carboxylesterase activity in Trypanosoma cruzi was found mainly in the microsomal (40%) and the cytosolic fraction (26%). The Vmax for p-nitrophenyl acetate was 28.50 and 17.60 nmol per min and mg of protein for the microsomal and the cytosolic fractions, respectively.
J, Aldunate +3 more
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Biochemistry, 1969
The molecular weight of pig liver carboxylesterase (~88% pure) has been determined as 163,000 (±15,000). The enzyme has two active sites per molecular weight of 163,000 as shown by titration with pnitrophenyl dimethylcarbamate and p-nitrophenyl diethyl phosphate.
Horgan, Douglas J. +4 more
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The molecular weight of pig liver carboxylesterase (~88% pure) has been determined as 163,000 (±15,000). The enzyme has two active sites per molecular weight of 163,000 as shown by titration with pnitrophenyl dimethylcarbamate and p-nitrophenyl diethyl phosphate.
Horgan, Douglas J. +4 more
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Journal of Biochemistry, 2010
A novel gene encoding an esterase from Geobacillus thermodenitrificans strain CMB-A2 was cloned, sequenced and functionally expressed in Escherichia coli M15. Sequence analysis revealed an open reading frame of 747 bp corresponding to a polypeptide of 249 amino acid residues (named EstGtA2).
David M, Charbonneau +2 more
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A novel gene encoding an esterase from Geobacillus thermodenitrificans strain CMB-A2 was cloned, sequenced and functionally expressed in Escherichia coli M15. Sequence analysis revealed an open reading frame of 747 bp corresponding to a polypeptide of 249 amino acid residues (named EstGtA2).
David M, Charbonneau +2 more
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