منابع مشابه
Crystalline dihydroorotic dehydrogenase.
Evidence has previously been presented that dihydroorotic dehydrogenase from Zymobacterium oroticum (1) is a flavoprotein (2). The present paper describes a procedure for crystallizing the enzyme as a globulin. Data are also presented to show that the protein crystals contain about one atom of iron per molecule of flavin, and that the flavin consists of both flavin mononucleotide and flavin ade...
متن کاملEnzymes of the Pyrimidine Pathway in Escherichia Coli. Ii. Intracellular Localization and Properties of Dihydroorotic Dehydrogenase.
Taylor, W. Herman (Portland State College, Portland, Ore.), and Mary L. Taylor. Enzymes of the pyrimidine pathway in Escherichia coli. II. Intracellular localization and properties of dihydroorotic dehydrogenase. J. Bacteriol. 88:105-111. 1964.-Intracellular localization of three enzymes of the pyrimidine pathway in Escherichia coli was studied. Dihydroorotic dehydrogenase was found to be assoc...
متن کاملCrystalline Lactic Dehydrogenase of the Lens.
A protein with low LDH activity compared to recrystallized muscle LDH and one which appeared to be homogeneous by all available tests for protein homogeneity has been obtained in crystalline form from bovine and rabbit lenses. These lens LDH preparations appeared to be identical immunologically in the other mammalian species examined. The bovine lens LDH had half the molecular weight of LDH iso...
متن کامل58. Crystalline Lactic Dehydrogenase from Heart Muscle
THE reduction of methylene blue by lactic acid, or in other words, the dehydrogenation of lactic acid in the presence of extracts from animal tissues, is now known to be catalysed by a system composed of two enzymes (lactic dehydrogenase and diaphorase flavoprotein) and cozymase [Dewan & Green, 1938; Euler & Hellstrom, 1938]. The chemical reactions involved in this process may be written [Corra...
متن کاملCrystalline glycerophosphate dehydrogenase from rabbit muscle.
Enzymatic activity was determined in an optical test, based on the measurement of reduced DPN at 340 rnp in the Beckman spectrophotometer. The reaction was carried out in phosphate or cysteine buffer at pH 7. Synthetic dihydroxyacetone phosphate (5) with reduced DPN or racemic cr-glycerophosphate with DPN was used as substrate to measure the forward and backward reactions, respectively. The con...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1960
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69438-4