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
Polychlorinated Biphenyls: A New Type of Inducer of Cytochrome P-448 in the Liver
TL;DR: The data suggest that Aroclor 1254-induced cytochrome P-448 may be catalytically different from the 3-methylcholanthrene-induced P- 448 or that the hemoprotein(s) induced by Aro clonal 1254 may be a mixture of cytochromes P-447 and P-450 exhibiting catalytic properties of both cyto Chromes.
Journal ArticleDOI
Substrate-inducible Microsomal Aryl Hydroxylase in Mammalian Cell Culture: II. Cellular responses during enzyme induction
TL;DR: These studies suggest that the induction of aryl hydroxylase activity involves an activation of specific genes and changes in their transcription into messenger RNA.
Journal ArticleDOI
Oxidative inactivation of cytochrome P-450 1A (CYP1A) stimulated by 3,3',4,4'-tetrachlorobiphenyl: production of reactive oxygen by vertebrate CYP1As.
TL;DR: The results indicate that TCB uncouples the catalytic cycle of CYP1A, ostensibly CYP 1A1, resulting in formation of ROS within the active site, which may contribute to the toxicity of planar halogenated aromatic hydrocarbons.
Journal ArticleDOI
CYP2C9 Ile359 and Leu359 variants: enzyme kinetic study with seven substrates.
TL;DR: The results indicate that the Ile359 to Leu359 change significantly decreases the catalytic activity of all the CYP2C9-mediated metabolisms studied, whereas the extent of the reduction in activity and changes of the kinetic parameters varies between substrates.
Journal ArticleDOI
A Serine-Substituted P450 Catalyzes Highly Efficient Carbene Transfer to Olefins In Vivo
Pedro S. Coelho,Z. Jane Wang,Maraia E. Ener,Stefanie A. Baril,Arvind Kannan,Frances H. Arnold,Eric M. Brustad +6 more
TL;DR: A unique serine-heme ligated cytochrome “P411” that catalyzes efficient and selective carbene transfers from diazoesters to olefins in intact Escherichia coli cells is designed.
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