NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from porcine kidney. I. Purification and partial characterization. 1980

D T Kung-Chao, and H H Tai

The cytoplasmic NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (11 alpha, 15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, EC 1.1.1.141) from porcine kidney was purified to a specific activity of 1.2 unit per mg protein by a series of chromatographic techniques including affinity chromatography. The native molecular weight of the enzyme was estimated to be 45 000. Substrate specificity studies indicated that the enzyme was NAD+-specific and was able to catabolize readily various prostaglandins, with the exception of prostaglandin B and thromboxane B. The enzyme was inhibited by sulfhydryl inhibitors, diuretic drugs and various fatty acids.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D004232 Diuretics Agents that promote the excretion of urine through their effects on kidney function. Diuretic,Diuretic Effect,Diuretic Effects,Effect, Diuretic,Effects, Diuretic
D006911 Hydroxyprostaglandin Dehydrogenases Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins. Hydroxyprostaglandin Dehydrogenase,Prostacyclin Dehydrogenase,Dehydrogenase, Hydroxyprostaglandin,Dehydrogenase, Prostacyclin,Dehydrogenases, Hydroxyprostaglandin
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D013439 Sulfhydryl Reagents Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling. SH-Reagents,Sulfhydryl Compound Antagonists,Sulfhydryl Compound Inhibitors,Thiol Reagents,Sulfhydryl Compounds Antagonists,Sulfhydryl Compounds Inhibitors,Antagonists, Sulfhydryl Compound,Antagonists, Sulfhydryl Compounds,Compound Antagonists, Sulfhydryl,Compound Inhibitors, Sulfhydryl,Inhibitors, Sulfhydryl Compound,Inhibitors, Sulfhydryl Compounds,Reagents, Sulfhydryl,Reagents, Thiol,SH Reagents
D013552 Swine Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA). Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog

Related Publications

D T Kung-Chao, and H H Tai
February 1987, Prostaglandins, leukotrienes, and medicine,
D T Kung-Chao, and H H Tai
June 1993, Hua xi yi ke da xue xue bao = Journal of West China University of Medical Sciences = Huaxi yike daxue xuebao,
D T Kung-Chao, and H H Tai
August 1980, The Journal of biological chemistry,
D T Kung-Chao, and H H Tai
February 1979, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society,
D T Kung-Chao, and H H Tai
April 1987, Nihon Sanka Fujinka Gakkai zasshi,
D T Kung-Chao, and H H Tai
January 1982, Methods in enzymology,
Copied contents to your clipboard!