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- W1520181644 abstract "1. In the investigation of NAD glycohydrolase (EC 3.2.2.5) in the small intestine of the rat, the properties of this enzyme solubilized by lipase (glycerol-ester hydrolase, EC 3.1.1.3) and purified 250-fold were found to be similar in essentials to its properties found in other tissues. The Km values for NAD and NADP were 2.7·10−5 and 3.8·10−6 M, respectively. 2. An over 70% inhibition of NAD hydrolysis was observed in the presence of less than 1·10−6 M NADP when NAD was used at a concentration of 6.25·10−6 M as substrate. In contrast to the NADP effect on the NAD cleavage, a slight effect of NAD on the hydrolysis of the NADP was observed. 3. The permeability of pyridine nucleotide in the small intestine was studied. No penetration of [14C]NAD prior to degradation to [14C]nicotinamide was observed. This result would indicate that NAD glycohydrolase may contribute to the absorption of the pyridine moiety of NAD, which would be found significant in the diet." @default.
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- W1520181644 title "NAD glycohydrolase from the small intestine of the rat" @default.
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- W1520181644 doi "https://doi.org/10.1016/0005-2744(72)90346-4" @default.
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