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Open AccessJournal ArticleDOI

The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE

Tsuneo Omura, +1 more
- 01 Jul 1964 - 
- Vol. 239, Iss: 7, pp 2370-2378
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.
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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.

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Citations
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Journal ArticleDOI

Biochemical changes in rat liver after administration of carbon disulphide, with particular reference to microsomal changes

TL;DR: The most likely interpretation for these findings is that CS2 causes a rapid alteration in the cytochrome P-450 leading to loss of its spectrum and of its activity in drug oxidation and that the altered Cytochrome (or its haem moiety) is lost from the damaged membranes at a slow rate.
Journal ArticleDOI

Purification of hepatic microsomal cytochromes P-450 from β-naphthoflavone-treated Atlantic cod (Gadus morhua), a marine teleost fish

TL;DR: Four isozymes of cytochrome P-450 were purified to varying degrees of homogeneity from liver microsomes of cod, a marine teleost fish, and showed differences in the rate and optimal pH for conversion of this substrate, and in optical properties.
Journal ArticleDOI

Genetic analysis of factors controlling high-level expression of cytochrome P450, CYP6D1, cytochrome b5, P450 reductase, and monooxygenase activities in LPR house flies, Musca domestica.

TL;DR: Examination of microsomal monooxygenases in insecticide-susceptible and pyrethroid-resistant house fly strains found that increased expression of CYP6D1 in the LPR strain is both cis regulated by a factor(s) on autosome 1 and transregulated by a factors on autosomes 2, which supports previous claims that CYP 6D1 is responsible for Monooxygenase-mediated resistance in theLPR strain.
Journal ArticleDOI

Taxol Biosynthesis: Molecular Cloning and Characterization of a Cytochrome P450 Taxoid 7β-Hydroxylase

TL;DR: Kinetic and binding assays indicated selectivity of the 7 beta-hydroxylase for polyoxygenated and acylated taxoid substrates, an observation consistent with the operation of this enzyme in the central portion of the Taxol biosynthetic pathway.
Journal ArticleDOI

Isolation of rat liver microsomes by gel filtration

TL;DR: A method was developed for the rapid isolation of liver microsomes by means of gel filtration, which has the main advantages over conventional techniques, the considerable decrease of time required for isolation of the microsome, the improved removal of solutes like hemoglobin, and the improved suspension stability of the preparation.
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

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.

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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