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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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Book ChapterDOI

Bioconcentration, bioaccumulation, and metabolism of pesticides in aquatic organisms.

TL;DR: This chapter provides an overview of the enzymes that are capable of metabolizing or otherwise assisting in the removal of xenobiotics from aquatic species and their roles in ecotoxicological assessment.
Journal ArticleDOI

Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes.

TL;DR: Reconstitution in lipid micelles showed that CYP79D1 has a higher k(c) value with L-valine as substrate than withL-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava.
Journal ArticleDOI

On the inhibitory action of mersalyl on microsomal drug oxidation: a rigid organization of the electron transport chain.

TL;DR: Studies on the pattern of inhibition suggest a rigid electron-transport system linking a single molecule of TPNH-cytochrome c reductase to a number of molecules of cytochrome P-450 contained within a multicomponent complex and that reducing equivalents can be transferred only within a single enzyme complex with no demonstrable electron transfer interactions between the components of different complexes.
Journal ArticleDOI

CYP-specific bioactivation of four organophosphorothioate pesticides by human liver microsomes.

TL;DR: The data indicated that CYP1A2 and 2B6 are suggested as possible metabolic biomarkers of susceptibility to OPT toxic effect at the actual human exposure levels, while the role of CYP3A4 is more significant to the low-affinity component of OPT bioactivation.
Journal Article

Identification of cytochrome P-450 isoforms responsible for cis-tramadol metabolism in human liver microsomes.

TL;DR: It is demonstrated that cis-tramadol can be metabolized to tramadol metabolites M1, M2, M3, and M5 in human liver microsomal preparations.
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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