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Titlebook: Cytochrome P450; John B. Schenkman,Helmut Greim Book 1993 Springer-Verlag Berlin Heidelberg 1993 biosynthesis.cytochrome P450.enzyme.enzym

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發(fā)表于 2025-3-21 18:38:17 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Cytochrome P450
編輯John B. Schenkman,Helmut Greim
視頻videohttp://file.papertrans.cn/243/242611/242611.mp4
叢書名稱Handbook of Experimental Pharmacology
圖書封面Titlebook: Cytochrome P450;  John B. Schenkman,Helmut Greim Book 1993 Springer-Verlag Berlin Heidelberg 1993 biosynthesis.cytochrome P450.enzyme.enzym
描述In this book the editors have brought together the widest group of investigators of the cytochrome P450 superfamily in order to present complete and right up-to-date coverage of this important enzyme system. The authors describe and analyze the components of the enzyme system, the reaction mechanisms involved, and the evolution and nomenclature of this superfamily of enzymes. They also describe the hepatic microsomal enzyme in a large number of species, from mammalian to birds and fish, to plants and unicellular organisms. The different P450 forms in different tissues of the mammalian system are also treated. Regulatory factors of P450 expression receive considerable attention, as do studies on the mechanism of interaction of the microsomal monooxygenase system components. Of particular interest to the reader are, for the first time, a compilation of chapters dedicated to forms of cytochrome P450 involved in steroid hormone biosynthesis. This volume presents the most complete survey of the cytochrome P450 field. It will allow recognition and understanding of the very wide implications this enzyme system has on life processes.
出版日期Book 1993
關(guān)鍵詞biosynthesis; cytochrome P450; enzyme; enzymes; hormone; hormones; steroid; synthesis
版次1
doihttps://doi.org/10.1007/978-3-642-77763-9
isbn_ebook978-3-642-77763-9Series ISSN 0171-2004 Series E-ISSN 1865-0325
issn_series 0171-2004
copyrightSpringer-Verlag Berlin Heidelberg 1993
The information of publication is updating

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https://doi.org/10.1007/978-981-13-7693-1for this enzyme was prompted by the previous discovery of an NADPH-cytochrome . reductase in yeast (. et al. 1940). The yeast enzyme was shown to use NADPH as the source of reducing equivalents, and contained flavin mononucleotide (FMN) as a prosthetic group. This newly discovered enzyme was isolate
板凳
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https://doi.org/10.1007/978-981-16-1982-3ent of the microsomal mixed function oxidase system, functioning in the endoplasmic reticulum (. and . 1962; . and . 1962) and nuclear membrane (. 1971) to catalyze electron transfer from NADPH to cytochrome P450 (. and . 1968). This 78-kDa flavin mononucleotide (FMN)- and flavin adenine dinucleotid
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Combinatorial chemistry: A perspectivenzymatically active system was established by the use of phosphatidylcholines by . et al. (1970). Among various acyl derivatives of glycerol-3-phosphorylcholine the dioleoyl-derivative was most effective. The most commonly used and convenient system for reconstitution in numerous studies over the ye
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Annual Review of Gerontology and Geriatricstes include both xenobiotics (drugs, carcinogens, environmental pollutants, and other chemicals) and endogenous metabolites (steroids, fatty acids, prostaglandins, etc.). As shown in Fig. 1, the major sites of cytochrome P450 action in mammalian metabolism are reactions connected to sterol metabolis
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Depression in Late Life: An Updateated oxygen, representing oxygen metabolites, mainly reduction products of oxygen, released from the cytochrome P-450 enzyme system. Reactive oxygen formed during the metabolic reaction of the cytochrome P-450 enzyme at the active site of the heme moiety will not be discussed here; the reader is ref
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