Purification of the nicotinic acid hydroxylase system of Pseudomonas fluorescens KB1
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چکیده
منابع مشابه
The hydroxylation of nicotinic acid by Pseudomonas fluorescens.
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متن کاملThe oxidation of nicotinic acid by Pseudomonas fluorescens.
Morgan, W. T. J. & Elson, L. A. (1934). Biochem. J. 28,988. Morgan, W. T. J. & Partridge, S. M. (1940). Biochem. J. 34, 169. Morgan, W. T. J. & Partridge, S. M. (1941a). Biochem. J. 35, 1140. Morgan, W. T. J. & Partridge, S. M. (1941 b). Chem. & Ind. 60, 722. Partridge, S. M. (1948). Biochem. J. 42, 251. Partridge, S. M. & Morgan, W. T. J. (1940). Brit. J. exp. Path. 21, 180. Sevag, M. G. (1934...
متن کاملNicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.
An enzyme that catalyzes the reversible hpdroxylation of nicotinic acid to 6-hydroxynicotinic acid has been purified from extracts of a nicotinic acid-fermenting clostridium. The enzyme appears to be a flavin adenine dinucleotidecontaining non-heme iron protein and utilizes triphosphopyridine nucleotide as the ultimate electron acceptor. The purified enzyme also exhibits reduced triphosphopyrid...
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چکیده ندارد.
15 صفحه اولD-amino acid dehydrogenases of Pseudomonas fluorescens.
Two distinct D-amino acid dehydrogenases, each showing absolute speci&ity for methylene blue or 2,6-dichloroindophenol, respectively, were isolated from Pseudomonas @orescens (ATCC 11299B). The methylene blue-specific ~-amino acid dehydrogenase was detectable only in extracts from D-tryptophan-grown cells and was purified about 40-fold. The 2,6-dichloroindophenol-specif?c ~-amino acid dehydroge...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1959
ISSN: 0306-3283
DOI: 10.1042/bj0720001