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Time Course of Induction of Cytochrome P-450, NADPH-Cytochrome c Reductase, and Cinnamic Acid Hydroxylase by Phenobarbital, Ethanol, Herbicides, and Manganese in Higher Plant Microsomes
Author(s) -
Danièle WerckReichhart,
JeanPierre Salaün,
Irène Benveniste,
Francis Durst
Publication year - 1980
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.66.4.600
Subject(s) - chemistry , cytochrome , phenobarbital , microsome , reductase , cytochrome c peroxidase , biochemistry , ethanol , cytochrome c oxidase , cytochrome c , cinnamic acid , enzyme , mitochondrion , biology , pharmacology
The mixed function oxidase trans-cinnamic acid 4-hydroxylase, cytochrome P-450, cytochrome b(5), and NADPH-cytochrome c (P-450) reductase were measured in microsomes from aging artichoke tuber slices exposed to manganese, ethanol, phenobarbital, and the herbicides Chloro-IPC, Dichlobenil, and Monuron. Although the microsomal hydroxylating complex is already induced by the slicing and aging process, 25 millimolar MnCl(2), 4 millimolar phenobarbital, and 300 millimolar ethanol caused a marked increase of hydroxylase activity and cytochrome P-450 content and shifted their time course. The herbicides, 200 micromolar Dichlobenil and 200 micromolar Monuron, were less effective. Chloro-IPC was slightly inhibitory. NADPH cytochrome c reductase was significantly increased only in phenobarbital-treated slices. Cytochrome b(5) was generally the least affected among the parameters being measured. The mechanisms by which these compounds increase cytochrome P-450 content and hydroxylase activity are not yet defined.

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