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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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Enhancement of reactive oxygen-dependent mitochondrial membrane lipid peroxidation by the anticancer drug adriamycin

TL;DR: It is found that NADH-dependent mitochondrial peroxidation--measured by the 2-thiobarbituric acid method--was stimulated by adriamycin as much as 4-fold, and that in submitochondrial particles freed of endogenous defenses against oxyradicals, lipidperoxidation was increased 7-fold by adRIamycin.
Journal ArticleDOI

The effect of cimetidine on in vitro and in vivo microsomal drug metabolism in the rat

TL;DR: It is demonstrated that cimetidine is an in vitro inhibitor of microsomal drug metabolism in the rat and this inhibition leads to pharmacokinetic drug-drug interactions in vivo.
Journal Article

Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P-450 2C8 and P-450 3A4 in human liver microsomes.

TL;DR: The results suggest that in human liver both CYP2C8 and CYP3A4 have major roles in quinone-type metabolite formation and that the hepatic contents of these two P- 450 forms determine which P-450 enzymes play major role in individual humans.
Journal Article

Metabolic Oxidation of Carcinogenic Arylamines by Rat, Dog, and Human Hepatic Microsomes and by Purified Flavin-containing and Cytochrome P-450 Monooxygenases

TL;DR: The hypothesis that 1-NA is probably not carcinogenic is supported, as carcinogenic arylamines appear to be metabolized similarly in humans and experimental animals and perhaps selectively by a specific form of hepatic cytochrome P-450.
Journal Article

Presence and Activity of Cytochrome P450 Isoforms in Minipig Liver Microsomes: Comparison with Human Liver Samples

TL;DR: The results indicate that minipigs might be, in many cases, the most suitable experimental animals to predict biotransformation pathways in humans, because the activity of the most important CYP isoform in humans (CYP3A, metabolizing the majority of known drug substrates) is present in minipig liver microsomes, with comparable levels and activities.
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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