Bovine Liver Formaldehyde Dehydrogenase
نویسندگان
چکیده
منابع مشابه
A comparison of rat and human liver formaldehyde dehydrogenase.
An NADand GSH-dependent formaldehyde dehydrogenase (formaldehyde: NAD* oxidoreductase, EC 1.2.I.Z) was purified from rat and human liver, and the properties of these enzymes were compared. The GSH requirement of the enzyme obtained from both species could not be replaced by dithiothreitol, CoA or cysteine, and NADP could not substitute for NAD. The pH optimum, and the Km of formaldehyde and NAD...
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The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...
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In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
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Reports from various laboratories have dealt with the binding properties of glutamate dehydrogenase from bovine liver (EC 1.4.1.3) (Pantaloni & Dessen, 1969; Huang & Frieden, 1969; Malcolm, 1972; Brown et al., 1973; Koberstein & Sund, 1973), but unfortunately these reports differ considerably over the number and nature of glutamate dehydrogenase coenzyme-binding sites as well as the magnitude o...
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1. Initial rates of oxidative deamination of L-glutamate with NAD+ as coenzyme, and of reductive aminiation of 2-oxoglutarate with NADH as coenzyme, catalysed by bovine liver glutamate dehydrogenase were measured in 0.111 M-sodium phosphate buffer, pH 7, at 25 degrees C, in the absence and presence of product inhibitors. All 12 possible combinations of variable substrate and product inhibitor w...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)71505-6