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Hydroperoxide-dependent hydroxylation involving "H2O2-reducible hemoprotein" in microsomes of pea seeds. A new type enzyme acting on hydroperoxide and a physiological role of seed lipoxygenase.

作者信息

Ishimaru A, Yamazaki I

出版信息

J Biol Chem. 1977 Sep 10;252(17):6118-24.

PMID:19466
Abstract
摘要

相似文献

1
Hydroperoxide-dependent hydroxylation involving "H2O2-reducible hemoprotein" in microsomes of pea seeds. A new type enzyme acting on hydroperoxide and a physiological role of seed lipoxygenase.豌豆种子微粒体中涉及“可被过氧化氢还原的血红蛋白”的过氧化氢依赖性羟基化作用。一种作用于过氧化氢的新型酶及种子脂氧合酶的生理作用。
J Biol Chem. 1977 Sep 10;252(17):6118-24.
2
The carbon monoxide-binding hemoprotein reducible by hydrogen peroxide in microsomal fractions of pea seeds.
J Biol Chem. 1977 Jan 10;252(1):199-204.
3
Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P-450.
Arch Biochem Biophys. 1976 Aug;175(2):524-33. doi: 10.1016/0003-9861(76)90541-5.
4
Induction of microsomal aryl hydrocarbon (3,4-benzo(alpha)pyrene) hydroxylase and cytochrome P-450K in rat kidney cortex. II. Interactions with the induced hemoprotein.
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Involvement of cytochrome P-450 in the intracellular formation of lipid peroxides.
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Purification and characterization of solubilized peroxygenase from microsomes of pea seeds.
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Hydroperoxide catalyzed liver microsomal aromatic hydroxylation reactions involving cytochrome P-450.
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8
Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo- and flavoprotein domains.
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Prolonged depression of hepatic microsomal drug metabolism and hemoprotein levels following a single dose of 1-(2-chloroethyl)-3-cyclohexyl-1-nitrosourea (CCNU).
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[Inactivation of cytochrome P-450 by hydrogen peroxide formed in the catalytic cycle during peroxy-complex degradation].
Biokhimiia. 1989 Jul;54(7):1102-7.

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