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
Conversion of P-450 to P-420 by Neutral Salts and some other Reagents
Y. Imai,Ryuichiro Sato +1 more
TL;DR: The structure around the heme group of P-450 as well as the mechanism of its conversion to P-420 are discussed, and iodine was an effective conversion agent that caused considerable destruction of the hemoprotein.
Journal Article
The Preparation of Microsomal Fractions of Rodent Respiratory Tract and Their Characterization
TL;DR: A method for preparing rodent lung microsomes using normal differential centrifugation methods is described which allows the spectral characterization of these lung fractions, which appear to use reduced nicotinamide adenine dinucleotide more effectively as an electron donor to reduce cytochrome P-450 than do liver microsomal fractions.
Journal Article
Metabolism and Transport of the Macrolide Immunosuppressant Sirolimus in the Small Intestine
TL;DR: Intestinal drug metabolism and countertransport into the gut lumen, drug interactions with CYP3A substrates and inhibitors in the small intestine and an 8-fold interindividual variability of the intestinal metabolite formation rate significantly contribute to the low and highly variable bioavailability of sirolimus.
Journal ArticleDOI
Mechanism of induction of hepatic microsomal drug metabolizing enzymes by a series of barbiturates.
Costas Ioannides,Dennis V. Parke +1 more
TL;DR: Barbitone is an effective inducer of the drug‐metabolizing enzymes, yet does not interact spectrally with cytochrome P‐450; this is in accord with the observations that although there are increases in NADPH‐cytochrome c reductase and cy tochrome b5, following administration of barbitone there is no increase in cyto Chrome P‐ 450.
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