Compounds > 15-ketoprostaglandin-f2alpha

15-ketoprostaglandin-f2alpha and quercitrin

15-ketoprostaglandin-f2alpha has been researched along with quercitrin* in 1 studies

Other Studies

1 other study(ies) available for 15-ketoprostaglandin-f2alpha and quercitrin

Article	Year
Purification of a 15-ketoprostaglandin delta 13-reductase from rat liver and its ability to reduce the double bond of xenobiotics. Biochemistry and molecular biology international, 1993, Volume: 30, Issue:5 A 15-ketoprostaglandin delta 13-reductase was purified to homogeneity from rat liver. The enzyme used NADPH much more effectively than NADH as an electron donor. The molecular weight was estimated to be 39,500 by electrophoresis and 42,000 by gel filtration. The Km apparent for 15-ketoprostaglandin F2 alpha was 213 nM. The enzyme was markedly inhibited by dicumarol, quercitrin, p-chloromercuribenzoic acid and indomethacin. The enzyme had an isoelectric point at pH 4.5 and a broad pH optimum. The enzyme also exhibited the double bond reductase activity toward several xenobiotics with the double bond adjacent to the carbonyl group. Topics: 15-Oxoprostaglandin 13-Reductase; Animals; Chloromercuribenzoates; Cytosol; Dicumarol; Dinoprost; Hydrogen-Ion Concentration; Indomethacin; Isoelectric Focusing; Liver; Male; Molecular Weight; NAD; NADP; Oxidation-Reduction; p-Chloromercuribenzoic Acid; Quercetin; Rats; Rats, Wistar; Xenobiotics	1993

Article

Year

Purification of a 15-ketoprostaglandin delta 13-reductase from rat liver and its ability to reduce the double bond of xenobiotics.

Biochemistry and molecular biology international, 1993, Volume: 30, Issue:5

A 15-ketoprostaglandin delta 13-reductase was purified to homogeneity from rat liver. The enzyme used NADPH much more effectively than NADH as an electron donor. The molecular weight was estimated to be 39,500 by electrophoresis and 42,000 by gel filtration. The Km apparent for 15-ketoprostaglandin F2 alpha was 213 nM. The enzyme was markedly inhibited by dicumarol, quercitrin, p-chloromercuribenzoic acid and indomethacin. The enzyme had an isoelectric point at pH 4.5 and a broad pH optimum. The enzyme also exhibited the double bond reductase activity toward several xenobiotics with the double bond adjacent to the carbonyl group.

Topics: 15-Oxoprostaglandin 13-Reductase; Animals; Chloromercuribenzoates; Cytosol; Dicumarol; Dinoprost; Hydrogen-Ion Concentration; Indomethacin; Isoelectric Focusing; Liver; Male; Molecular Weight; NAD; NADP; Oxidation-Reduction; p-Chloromercuribenzoic Acid; Quercetin; Rats; Rats, Wistar; Xenobiotics

1993