The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE
Tsuneo Omura,Ryo Sato +1 more
TLDR
The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.About:
This article is published in Journal of Biological Chemistry.The article was published on 1964-07-01 and is currently open access. It has received 11895 citations till now. The article focuses on the topics: Carbon monoxide binding & Microsome.read more
Citations
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Drug metabolism by Escherichia coli expressing human cytochromes P450.
TL;DR: Transformed bacteria metabolized a number of typical P450 substrates at levels comparable to isolated bacterial membranes fortified with an NADPH-generating system, and compare favorably with those obtained using human liver microsomes as well as those of reconstituted in vitro systems composed of purified proteins, lipids, and cofactors.
Journal ArticleDOI
The antiaggregating activity of clopidogrel is due to a metabolic activation by the hepatic cytochrome P450-1A.
Pierre Savi,J. Combalbert,Gaich C,Rouchon Mc,Jean-Pierre Maffrand,Y. Berger,Jean-Marc Herbert +6 more
TL;DR: The efficacy of clopidogrel was increased in animals pretreated with 3-methylcholanthrene and beta-naphthoflavone, indicating that the cytochrome P450-1A subfamily pathway was mainly involved in the activating metabolism of clobidog rel, and the use of specific antibodies directed against the various cyto Chrome P450 subfamilies ascertained this observation.
Journal Article
Sudan I Is a Potential Carcinogen for Humans Evidence for Its Metabolic Activation and Detoxication by Human Recombinant Cytochrome P450 1A1 and Liver Microsomes
TL;DR: A carcinogenic potency of this rodent carcinogen for humans is strongly suggested by the first report on the metabolism of Sudan I by human CYP enzymes, which found that human microsomes were competent in activating Sudan I to form adducts with DNA.
Journal ArticleDOI
Metabolism of benzo[a]pyrene and benzo[a]pyrene-7,8-diol by human cytochrome P450 1B1.
James H. Kim,Kevin H. Stansbury,Nigel J. Walker,Michael A. Trush,Paul T. Strickland,Thomas R. Sutter +5 more
TL;DR: The results of these studies indicate that cytochrome P450 1B1 carries out metabolism of B[a]P along the pathway to the postulated ultimate carcinogen, the diol epoxide 2, at rates much higher than P 450 1A2 but less than P4501A1.
Journal ArticleDOI
Kinetic parameters of drug-metabolizing enzymes in Ca2+-sedimented microsomes from rat liver☆
TL;DR: Kinetic parameters of five substrates of the mixedfunction oxidase system were determined to ensure that the mixed function oxidases were unaltered by the Ca 2+ -sedimented microsomes.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI
The Carbon Monoxide-binding Pigment of Liver Microsomes II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES
Tsuneo Omura,Ryo Sato +1 more
TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.
Journal ArticleDOI
Hepatic Triphosphopyridine Nucleotide-Cytochrome c Reductase: Isolation, Characterization, and Kinetic Studies
TL;DR: Evidence is presented which suggests that this enzyme participates in a microsomal elect,ron transport system which does not include cytochrome c and kinetic evidence has been obtained which allows certain conclusions to be drawn concerning the mechanism of catalysis by this enzyme.
Journal ArticleDOI
Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.
Charles Williams,Henry Kamin +1 more
TL;DR: The biological role of reduced triphosphopyridine nucleotide (TPNH) and the metabolic pathways of its hydrogen atom and electron appear to be fundamentally different from those of reduced diphosphipyridineucleotide (DPNH).
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The Carbon Monoxide-binding Pigment of Liver Microsomes II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES
Tsuneo Omura,Ryo Sato +1 more