Glutamate dehydrogenase of nuclear and extra-nuclear compartments of Chang's liver cells.
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Amino Acids↗
Biomedical subjects
G Di Prisco
Publications and source records attributed to G Di Prisco.
Amino and aromatic groups in enzymic catalysis.
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Alkylation↗
Effects of phosphate and other ionic compounds on the activity of crystalline beef liver glutamate dehydrogenase.
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Adenine Nucleotides↗
Desensitization of the allosteric sites of glutamate dehydrogenase by fluorodinitrobenzene.
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Adenine Nucleotides↗
Purification and properties of a soluble reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase from the hepatopancreas of Octopus vulgaris.
1. The oxidation of NADH and NADPH catalysed by the soluble supernatant from the hepatopancreas of Octopus vulgaris is due to a single enzyme, which has been purified approximately 100-fold. The enzyme reacts rapidly with potassium ferricyanide, and more slowly with 2,6-dichlorophenol-indophenol. No activity is obtained with oxygen, cytochrome c, lipoic acid, vitamin K(1), vitamin K(3), ubiquinone-30, p-benzoquinone, 2-p-iodophenyl-3-p-nitrophenyl-5-phenyltetrazolium chloride or methylene blue. 2. GSH, cysteine and mercaptoethanol stimulate the enzymic activity up to fivefold. GSSG is without any apparent effect. When stimulated by GSH the enzyme becomes sensitive to dicoumarol, which produces an inhibition competitive with respect to the activator. 3. The purified enzyme contains an acid-removable flavine component, which has been identified as FMN by spectrofluorimetry and chromatography in three solvent systems. After acid ammonium sulphate treatment the enzymic activity is lost, but it can be almost fully restored by incubation with FMN. FAD produces only a partial reactivation.
Animals↗