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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Journal ArticleDOI
Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site.
Magang Shou,James Grogan,J. A. Mancewicz,Kristopher W. Krausz,Frank J. Gonzalez,Harry V. Gelboin,Kenneth R. Korzekwa +6 more
TL;DR: Kinetic analyses of these two substrates show that 7,8-benzoflavone increases the Vmax of phenanthrene metabolism without changing the Km and that Phenanthrene decreases the V max of 7, 8-benZ oflavone metabolism without increasing the KM, providing the first evidence that two different molecules can be simultaneously bound to the same P450 active site.
Journal ArticleDOI
Phenotypic stability of adult rat hepatocytes in primary monolayer culture.
TL;DR: P phenotypic change occurs in primary hepatocyte culture, not only in mammalian but also in amphibian hepatocytes7; it is distinct from a process of senescence or impaired viability; and it may be quantitatively impressive, involving key hepatic functions.
Book ChapterDOI
Biochemistry of Drug Oxidation and Reduction by Enzymes in Hepatic Endoplasmic Reticulum
TL;DR: This chapter discusses the biochemistry of drug oxidation and reduction by enzymes in hepatic endoplasmic reticulum, and the pharmacological effects of highly bound drugs, such as chlorpromazine, phenylbutazone, and thiopental.
Journal ArticleDOI
Studies on the induction of CO-binding pigments in liver microsomes by phenobarbital and 3-methylcholanthrene.
Journal ArticleDOI
Arachidonic Acid-metabolizing Cytochrome P450 Enzymes Are Targets of ω-3 Fatty Acids
Cosima Arnold,Marija Markovic,Katrin Blossey,Gerd Wallukat,Robert Fischer,Ralf Dechend,Anne Konkel,Clemens von Schacky,Friedrich C. Luft,Friedrich C. Luft,Dominik N. Müller,Michael Rothe,Wolf-Hagen Schunck +12 more
TL;DR: It is found that these ω-3 epoxides are highly active as antiarrhythmic agents, suppressing the Ca2+-induced increased rate of spontaneous beating of neonatal rat cardiomyocytes, at low nanomolar concentrations.
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
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