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- W1472568302 abstract "Publisher Summary This chapter discusses Bacillus subtilis NADase and its specific protein inhibitor. nicotinamide adenine dinucleotide (NAD)ase catalyzes the hydrolysis of the nicotinamide-ribose bond in NAD + to yield nicotinamide and adenosine diphosphoribose. The NADase from B. subtilis and its protein inhibitor is, thus, far the only system that has been purified to homogeneity. The B. subtilis NADase as well as its specific inhibitor contain relatively large amounts of carbohydrate. The carbohydrate content of the enzyme is about 52.8%, whereas the inhibitor contains as much as 72.7% carbohydrate. Sialic acid appears to be absent in both the compounds. The molecular weight of the enzyme as well as of the inhibitor was found to be 26,200 by ultracentrifugation, whereas that of the enzyme-inhibitor complex was found to be 52,700. Considerably lower values are obtained when the molecular weights are determined by gel filtration that is probably due to the carbohydrate content of the two proteins. The B. subtilis NADase is quite specific for the oxidized coenzymes. NADP + is hydrolyzed at about half the rate of NAD + under assay conditions. Reduced coenzymes are not hydrolyzed by the enzyme and they do not inhibit the hydrolysis of the oxidized coenzymes. The enzyme appears to be very specific for the nicotinamide moiety of the coenzyme analogs." @default.
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- W1472568302 date "1980-01-01" @default.
- W1472568302 modified "2023-09-27" @default.
- W1472568302 title "[21] Bacillus subtilis NADase and its specific protein inhibitor" @default.
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- W1472568302 doi "https://doi.org/10.1016/0076-6879(80)66451-9" @default.
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