Zobrazeno 1 - 10
of 11
pro vyhledávání: '"C M, Ensor"'
Publikováno v:
The FASEB Journal. 36
Publikováno v:
Analytical Chemistry. 70:579A-585A
Reporter proteins can be used in bioanalytical methods to produce signals indicating the presence of a target analyte.
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 78:982-989
Type 1 15-hydroxyprostaglandin dehydrogenase (PGDH) is the main enzyme responsible for the metabolism of prostaglandin E2 (PGE2) and PGF2 alpha. To examine the possibility that a deficiency of PGDH might contribute to preterm labor, we measured local
Publikováno v:
Journal of Biological Chemistry. 268:16437-16442
Oxidation of many prostaglandins at C-15 results in the formation of 15-keto metabolites, which have reduced biological activity. This reaction is catalyzed by NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. Using the photoaffinity analog of
Publikováno v:
ChemInform. 29
Reporter proteins can be used in bioanalytical methods to produce signals indicating the presence of a target analyte.
Publikováno v:
Journal of Biological Chemistry. 265:14888-14891
NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase catalyzes the oxidation of many prostaglandins at C-15, resulting in a subsequent reduction in their biological activity. We report the isolation of the cDNA for this enzyme. A human placental la
Publikováno v:
Analytical chemistry. 70(17)
Autor:
C M, Ensor, H H, Tai
Publikováno v:
Methods in enzymology. 280
Autor:
Jennifer C. Ousey, Fernand Labrie, Nicola Holdstock, Abigail L. Fowden, Marian Silver, X. Han, P. D. Rossdale, C. M. Ensor, H-H. Tai, A. Belanger, John R. G. Challis, A. J. McGLADDERY, W. R. Allen
Publikováno v:
Equine veterinary journal. 27(5)
15-hydroxy prostaglandin dehydrogenase (PGDH) is the critical enzyme that determines metabolism of primary prostaglandins. Its expression is determined in part by steroid hormones, particularly progesterone, formed from delta(5) steroids through 3bet
Publikováno v:
The Journal of biological chemistry. 268(22)
Oxidation of many prostaglandins at C-15 results in the formation of 15-keto metabolites, which have reduced biological activity. This reaction is catalyzed by NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. Using the photoaffinity analog of