Results 251 to 260 of about 127,252 (263)
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Cytochrome P450 biosensors—a review
Biosensors and Bioelectronics, 2005Cytochrome P450 (CYP) is a large family of enzymes containing heme as the active site. Since their discovery and the elucidation of their structure, they have attracted the interest of scientist for many years, particularly due to their catalytic abilities.
Bistolas, Nikitas +3 more
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2007
Plants are sessile organisms that cannot avoid exposure to adverse climatic conditions or attack from herbivores and pests by escaping. To survive and protect themselves, they are dependent on the ability to (a) redirect their overall metabolism to meet environmental constraints, (b) construct physical barriers that are difficult to penetrate, (c ...
Nielsen, Kirsten Annette +1 more
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Plants are sessile organisms that cannot avoid exposure to adverse climatic conditions or attack from herbivores and pests by escaping. To survive and protect themselves, they are dependent on the ability to (a) redirect their overall metabolism to meet environmental constraints, (b) construct physical barriers that are difficult to penetrate, (c ...
Nielsen, Kirsten Annette +1 more
openaire +2 more sources
Spectral Analyses of Cytochromes P450
2003UV/Vis spectroscopy is the major means of identifying intact holocytochrome P450. The carbon monoxide complex of the intact ferrous hemoprotein exhibits a characteristic spectrum between 448 and 452 nm, considerably distinct from the usual Soret absorption peaks of hemoproteins.
John B. Schenkman, Ingela Jansson
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Cytochrome P450 Reconstitution Systems
2003Human liver microsomes contain multiple forms of cytochrome P450 (CYP or P450) that catalyze oxidation of a number of xenobiotic and endobiotic chemicals. Individual P450 forms have unique, but overlapping, substrate specificities. It is necessary to determine which P450s play more important roles in the oxidation of these chemicals.
Hiroshi Yamazaki, Tsutomu Shimada
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1991
Publisher Summary This chapter discusses the cytochrome P450 turnover. The hepatic microsomal hemoproteins, collectively termed as cytochrome P450, consist of a family of multiple isozymes, all of which recruit heme, as their essential prosthetic moiety. These hemoproteins are monomeric, containing one heme moiety per mole of enzyme.
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Publisher Summary This chapter discusses the cytochrome P450 turnover. The hepatic microsomal hemoproteins, collectively termed as cytochrome P450, consist of a family of multiple isozymes, all of which recruit heme, as their essential prosthetic moiety. These hemoproteins are monomeric, containing one heme moiety per mole of enzyme.
openaire +3 more sources
Journal of Lipid Mediators and Cell Signalling, 1995
Michal L. Schwartzman, John C. McGiff
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Michal L. Schwartzman, John C. McGiff
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Cytochrome P450 and atherosclerosis
Clinical Pharmacology & Therapeutics, 1996openaire +3 more sources