Results 141 to 150 of about 14,849 (185)
Some of the next articles are maybe not open access.
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
openaire +4 more sources
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
openaire +4 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Canadian Journal of Biochemistry, 1975
Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform–acetone); sheep, 200 mg from 400 g of powder ...
P A, Inkerman +5 more
openaire +2 more sources
Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform–acetone); sheep, 200 mg from 400 g of powder ...
P A, Inkerman +5 more
openaire +2 more sources
Drug Metabolism and Disposition, 2011
Human carboxylesterase (CES) 1 and CES2 are members of the serine hydrolase superfamily, and both exhibit broad substrate specificity and are involved in xenobiotic and endobiotic metabolism. Although expression of CES1 and CES2 occurs in several organs, their expression in liver and small intestine is predominantly attributed to CES1 and CES2 ...
Jie, Wang +4 more
openaire +2 more sources
Human carboxylesterase (CES) 1 and CES2 are members of the serine hydrolase superfamily, and both exhibit broad substrate specificity and are involved in xenobiotic and endobiotic metabolism. Although expression of CES1 and CES2 occurs in several organs, their expression in liver and small intestine is predominantly attributed to CES1 and CES2 ...
Jie, Wang +4 more
openaire +2 more sources
Biochemical and Biophysical Research Communications, 1975
During the final stage of purification of pig liver carboxylesterase on CM-Sephadex, several enzyme activities are present in addition to the pig liver carboxylesterase reported from this laboratory (Horgan et al., 1969a). Variation in substrate specificity and specific activity of the material isolated from CM-Sephadex has been analysed with four ...
Hamilton S.E. +3 more
openaire +4 more sources
During the final stage of purification of pig liver carboxylesterase on CM-Sephadex, several enzyme activities are present in addition to the pig liver carboxylesterase reported from this laboratory (Horgan et al., 1969a). Variation in substrate specificity and specific activity of the material isolated from CM-Sephadex has been analysed with four ...
Hamilton S.E. +3 more
openaire +4 more sources
Heterogeneity of carboxylesterases in rat liver cells
Biochemical Pharmacology, 1992Rat liver cells were separated into parenchymal cells (PC), Kupffer cells (KC) and endothelial cells (EC). The distribution of carboxylesterases (EC 3.1.1.1) between these cell types was investigated by PAGE and chromatogenic substrate staining, and compared with the results for total liver preparation and individual isoenzymes isolated by ...
R, Gaustad, T, Berg, F, Fonnum
openaire +2 more sources
[45] Carboxylesterases-amidases
1981Publisher Summary This chapter presents the simultaneous purification of five of the most prominent rat liver carboxylesterases-amidases. All of these enzymes are found in microsomal fraction. As a side product of the procedure described in the chapter , a dipeptidyl aminopeptidase is obtained that also belongs to the group of serine hydrolases.
Eberhard Heymann, Rolf Mentlein
openaire +1 more source
Carboxylesterases (EC 3.1.1). Dissociation of ox liver carboxylesterase
Biochemistry, 1969M T, Runnegar, E C, Webb, B, Zerner
openaire +2 more sources
Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase
Biochemistry, 1969Runnegar M.T.C. +3 more
openaire +3 more sources