Zobrazeno 1 - 10
of 52
pro vyhledávání: '"C B, Kasper"'
Publikováno v:
Brazilian Journal of Biology, Iss 0 (2018)
Abstract Between July 2014 and April 2015, we conducted weekly inventories of the circadian activity patterns of mammals in Passo Novo locality, municipality of Alegrete, southern Brazil. The vegetation is comprised by a grassy-woody steppe (grasslan
Externí odkaz:
https://doaj.org/article/9760903dab3d4f7b9368a4a7686db055
Publikováno v:
Brazilian Journal of Biology, Vol 76, Iss 1, Pp 228-232
Abstract Home range and minimal population densities of Southern tiger cat (Leopardus guttulus), margay (Lepardus wiedii) and jaguarundi (Puma yagouaroundi) were estimated between 2005 and 2006 in Taquari Valley, near the southern edge of the Atlanti
Externí odkaz:
https://doaj.org/article/3f8ee4925785476a8b53338b7eaa3b71
Publikováno v:
The Journal of biological chemistry. 276(31)
NADPH-cytochrome P450 oxidoreductase catalyzes transfer of electrons from NADPH, via two flavin cofactors, to various cytochrome P450s. The crystal structure of the rat reductase complexed with NADP(+) has revealed that nicotinamide access to FAD is
Autor:
P A, Bell, C B, Kasper
Publikováno v:
The Journal of biological chemistry. 268(19)
The cDNA containing the complete coding region for rat microsomal epoxide hydrolase (EC 3.3.2.3) was cloned into the expression/secretion vector pIN-III-OmpA3 and expressed in Escherichia coli strain TG1. Recombinant epoxide hydrolase was found to re
Autor:
A. L. Shen, C. B. Kasper
Publikováno v:
Cytochrome P450 ISBN: 9783642777653
The enzyme NADPH-cytochrome P450 oxidoreductase (NADPH: ferrihemoprotein oxidoreductase, E.C. 1.6.2.4, hereafter referred to as reductase) is a component of the microsomal mixed function oxidase system, functioning in the endoplasmic reticulum (Willi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08246a7315351ad9739e85e291f010bb
https://doi.org/10.1007/978-3-642-77763-9_3
https://doi.org/10.1007/978-3-642-77763-9_3
Publikováno v:
The Journal of biological chemistry. 266(30)
Site-directed mutagenesis was employed to investigate the role of Cys566 in the catalytic mechanism of rat liver NADPH-cytochrome P-450 oxidoreductase. Rat NADPH-cytochrome P-450 oxidoreductase and mutants containing either alanine or serine at posit
Publikováno v:
The Journal of biological chemistry. 266(8)
Intraperitoneal administration of lead acetate to male Sprague-Dawley rats resulted in the tissue-specific transcriptional activation of the microsomal epoxide hydrolase gene in kidney. This response was followed by a 15-fold increase in the level of
Publikováno v:
Cancer research. 50(24)
Mitomycin C is an alkylating agent used in cancer chemotherapy that shows some specificity towards hypoxic cells. The therapeutic effects of this compound are thought to result from its metabolic activation by enzymes such as NADPH:cytochrome P-450 r
Autor:
F J Gonzalez, C B Kasper
Publikováno v:
Journal of Biological Chemistry. 257:5962-5968
Publikováno v:
Journal of Biological Chemistry. 260:515-521
Filter-hybridization studies show that major phenobarbital and pregnenolone-16alpha-carbonitrile-inducible cytochrome P-450 mRNAs in rats were encoded by members of separate, distinct gene families. These gene families are genetically divergent from