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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Differential induction of rat liver microsomal UDP-glucuronosyltransferase activities by various inducing agents
TL;DR: In contrast to 3-methylcholanthrene-type inducers, ethoxyquin and trans-stilbene oxide markedly induced GT1 reactions without affecting benzo[a]pyrene monooxygenase.
Journal ArticleDOI
Metabolism of theophylline by cDNA-expressed human cytochromes P-450.
TL;DR: It is suggested that not only tobacco smoking but also chronic alcohol intake may influence theophylline elimination in man as ethanol induces CYP2E1, and the findings confirm the major role of CYP1A2 in theophyLLine metabolism and explain why in vivo the elimination kinetics of theophylla are non-linear and in vitro theophylliine metabolism by human liver microsomes does not obey monophasic kinetics.
Journal ArticleDOI
Toxicity and distribution of cadmium administered to rats at sublethal doses.
TL;DR: It appears that the redistribution of cadmium to the kidney with time is due to the longer time period required for the increase of metallothionein levels in the kidney.
Journal ArticleDOI
P450c17 mutations R347H and R358Q selectively disrupt 17,20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5
TL;DR: The data offer the first evidence that R347 is a crucial component of the site at which b5 interacts with the P450c17 x OR complex to promote electron transfer, and prove that the lyase activity was disrupted by interfering with electron transfer.
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Cytochrome P450 isoforms involved in metabolism of the enantiomers of verapamil and norverapamil
TL;DR: In this article, the enantiomers of verapamil and norverapamils were evaluated using a broad range of cytochrome P450 isoforms and measured the kinetic parameters of these processes.
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
Tsuneo Omura,Ryo Sato +1 more