Zobrazeno 1 - 10
of 74
pro vyhledávání: '"R. W. Estabrook"'
Publikováno v:
Biochemistry. Biokhimiia. 68(1)
To elucidate the nature of substrate specificity and intrinsic mechanism of hydroxylation of steroids, in the present work we carried out molecular cloning and heterologous expression of cDNA for three new forms of cytochrome P45017alpha from species
Publikováno v:
Journal of inorganic biochemistry. 87(4)
Cytochrome P450s (P450 or CYP) are the largest family of hemeproteins yet characterized. X-ray crystallographic studies have shown that the heme of the P450 hemeproteins is buried in the interior of the protein molecule. Unexplored are answers to que
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 25(11)
The antiandrogenic drug, flutamide, is widely used in the treatment of carcinoma of the prostate. The present study examines the metabolism of flutamide by human liver microsomes and purified recombinant human cytochrome P450s (CYP), expressed as fus
Publikováno v:
Methods in enzymology. 272
Publikováno v:
Methods in enzymology. 272
Autor:
A D, Rodrigues, D J, Mulford, R D, Lee, B W, Surber, M J, Kukulka, J L, Ferrero, S B, Thomas, M S, Shet, R W, Estabrook
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 23(7)
The metabolism of terfenadine was studied with a cDNA-expressed/purified recombinant fusion protein containing human liver microsomal cytochrome P4503A4 (CYP3A4) linked to rat NADPH-P450 reductase (rF450[mHum3A4/mRatOR]L1) and was compared with that
Publikováno v:
The Journal of biological chemistry. 267(15)
Cytochrome P-450BM-3 is a catalytically self-sufficient fatty acid omega-hydroxylase with two domains. Functional and primary structure analyses of the hemo- and flavoprotein domains of cytochrome P-450BM-3 and the corresponding microsomal cytochrome
Publikováno v:
FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 6(2)
Arachidonic acid and many products of the arachidonate cascade serve as substrates for cytochrome P450-mediated metabolism via allylic oxidation, omega hydroxylation, and epoxygenation as well as peroxide rearrangement. Defining the physiological imp
Publikováno v:
Current topics in cellular regulation. 33
Publikováno v:
Methods in enzymology. 206