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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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Role of Human Microsomal and Human Complementary DNA-expressed Cytochromes P4501A2 and P4503A4 in the Bioactivation of Aflatoxin B1

TL;DR: The results are consistent with the hypothesis that CYP1A2 is the high-affinity P450 enzyme principally responsible for the bioactivation of AFB1 at low substrate concentrations associated with dietary exposure.
Journal ArticleDOI

Liver-specific Deletion of the NADPH-Cytochrome P450 Reductase Gene: IMPACT ON PLASMA CHOLESTEROL HOMEOSTASIS AND THE FUNCTION AND REGULATION OF MICROSOMAL CYTOCHROME P450 AND HEME OXYGENASE *

TL;DR: The data indicate the absence of significant alternative redox partners for liver microsomal CYP and HO, provide in vivo evidence for the significance of hepatic CPR-dependent enzymes in cholesterol homeostasis and systemic drug clearance, and reveal novel regulatory pathways of CYP expression associated with altered cellularHomeostasis.
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Oxidative metabolism of the soy isoflavones daidzein and genistein in humans in vitro and in vivo.

TL;DR: Most of the oxidative metabolites of the hydroxylated daidzein and genistein metabolites in vivo are described as human in vivo metabolites for the first time and their biological significance remains to be established.
Journal ArticleDOI

On the mechanism of drug hydroxylation in rat liver microsomes.

TL;DR: It is concluded that the drug-hydroxylating enzyme system involves the microsomal TPNH-cytochrome c reductase and CO-binding pigment, and a hypothetic reaction scheme accounting for the data presented is proposed.
Journal ArticleDOI

The dietary control of the microsomal stearyl CoA desaturation enzyme system in rat liver.

TL;DR: The activity which had been decreased by starvation was rapidly induced to a very high level on refeeding of the animals and returned gradually to the steady-state level on continuation of feeding, suggesting that the dietary regulation involved the change of mainly the terminal component of the desaturation system, cyanide-sensitive factor.
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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