Results 131 to 140 of about 14,849 (185)

Human Liver Carboxylesterase. Properties and Comparison with Human Serum Carboxylesterase

The Journal of Biochemistry, 1983
Carboxylesterase was obtained from human liver in an electrophoretically homogeneous form. The monomeric molecular weight of the enzyme was 60,000 and the enzyme associated to form trimers. Purified human liver carboxylesterase was compared with human serum carboxylesterase, purified earlier.
T, Tsujita, H, Okuda
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Carboxylesterases (EC 3.1.1). Amino Acid Composition of Liver Carboxylesterases

Canadian Journal of Biochemistry, 1975
The amino acid compositions of the carboxylesterases from chicken, horse, ox, sheep, and pig livers are reported and compared. As would be expected for this homologous series, the compositions show a general similarity. However, there are some significant differences, but the degree to which particular pairs of enzymes differ is consistent with the ...
K, Scott, B, Zerner
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Carboxylesterases (EC 3.1.1.). A large-scale purification of pig liver carboxylesterase

Biochemistry, 1969
Two 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., Stoops, James K., Webb, Edwin C., Zerner, Burt   +3 more
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Structure, function and regulation of carboxylesterases

Chemico-Biological Interactions, 2006
This 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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Characterization of inhibitors of specific carboxylesterases: Development of carboxylesterase inhibitors for translational application

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, Janice L, Hyatt, Christopher L, Morton, Richard E, Lee, Philip M, Potter, Mary K, Danks   +5 more
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Carboxylesterases (EC 3.1.1). The Molecular Sizes of Chicken and Pig Liver Carboxylesterases

Canadian Journal of Biochemistry, 1975
The 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, 1967
Malaoxon 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, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
Atomi, H, Imanaka, T
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Enzymatic Activity of Human Carboxylesterases

Current Protocols in Toxicology, 2007
AbstractThe 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, 1987
Carboxylesterase 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, Y, Repetto, M E, Letelier, A, Morello   +3 more
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