THE JOURNAL OF VITAMINOLOGY
Online ISSN : 2185-2553
Print ISSN : 0022-5398
Partial Purification and Properties of Nicotinamide-Adenine Dinucleotide Nucleosidase and Interaction between Enzyme and Its Protein Inhibitor
NOBUO SUZUKI
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1968 Volume 14 Issue 2 Pages 121-128

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Abstract
1. About 400-fold purification was achieved from the crude heat-treated extract of M. butyricum.
2. The purified enzyme has a broad pH optimum and the Km value for NAD is 1.6×10-3M. This enzyme is quite insensitive to nicotinamide and isonicotinic acid hydrazide. PCMB shows no effect on the enzyme.
3. M. butyricum NADase cannot catalyze the transfer of isonicotinic acid hydrazide to the adenosine diphosphate ribose moiety of NAD.
4. A molecular weight of the purified enzyme was shown to be about 70, 000, while, for its protein inhibitor, about 20, 000 was obtained by Sephadex G-200 gel filtration.
5. The complex of NADase and its inhibitor was shown by Sephadex G-200 column.
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