Crystalline alcohol dehydrogenase from bakers' yeast
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This article is published in Journal of Biological Chemistry.The article was published on 1950-05-01 and is currently open access. It has received 584 citations till now. The article focuses on the topics: Alcohol dehydrogenase & Yeast.read more
Citations
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Journal ArticleDOI
The Carbon Monoxide-binding Pigment of Liver Microsomes I. EVIDENCE FOR ITS HEMOPROTEIN NATURE
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
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
TL;DR: The results are shown to favour the ferryl ion structure, or an isomer of this structure, for the higher oxidation state, and theHigher oxidation state may provisionally be named ferrylmyoglobin.
Book ChapterDOI
4 Lactate Dehydrogenase
TL;DR: This chapter discusses the lactate dehydrogenase, the only simpler dehydrogen enzyme where both structure and sequence are known at present.
Journal ArticleDOI
Studies on plasma membranes. i. chemical composition and enzyme content of plasma membranes isolated from rat liver
TL;DR: The possibility that the plasma-membrane preparations were contaminated by microsomal elements is discussed, and, on account of the available evidence, the conclusion is reached that there is no reason to assume that this was the case.
References
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Journal ArticleDOI
The mechanism of the oxidative reaction in fermentation
Otto Meyerhof,Peter Oesper +1 more
TL;DR: The findings confirm the conclusion drawn from other observations that the final values obtained represent true thermodynamic equilibria and show that the requirements of the law of mass action are excellently fulfilled for every component of the system at equilibrium.
Journal ArticleDOI
Über die Komponenten der Dehydrasesysteme. XII. Mechanismus der Dehydrierung von Alkohol und Triosephosphaten und der Oxydoreduktion.
Journal ArticleDOI
The role of the enzyme in the succinate-enzyme-fumarate equilibrium
Henry Borsook,Hermann F. Schott +1 more
TL;DR: An investigation into the role of the enzyme in the succinate-enzyme-fumarate equilibrium found the value of the free energy change in this reaction obtained from oxidation-reduction potentials was compared with that calculated from the entropies and other physicochemical properties of succinic acid and fumaric acid.
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