Characterization of the NAD+ glycohydrolase associated with the rat liver nuclear envelope.
The localization of NAD+ glycohydrolase [EC 3.2.2.5] (NADase) in purified rat liver nuclei has been examined. Subnuclear fractionation revealed that at least 70% of the NADase in nuclei was associated with the nuclear envelope fraction. The nuclear envelope fraction was practically free of microsomal contamination as judged by electron microscopic morphometry and assays of microsomal marker enzymes. Therefore, NADase was found to be an integral component of the nuclear envelope. The enzymological properties of the nuclear envelope NADase were compared with those of the microsomal enzyme. The nuclear envelope NADase was identical to the microsomal enzyme in its Km for NAD+ (60 muM), pH optimum (pH 6.5), ratio of transglycosidase activity to NADase activity (about 0.5), thermal stability and sensitivity to various inhibitors. Thus, NADase is a common enzymic component of both the nuclear envelope and the endoplasmic reticulum.
D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D009244:NAD+ Nucleosidase / Q000378:metabolism*; D009536:Niacinamide / Q000378:metabolism; D010743:Phospholipids / Q000032:analysis; D051381:Rats; D013696:Temperature
D010743:Phospholipids; D009243:NAD; D009536:Niacinamide; D009699:N-Glycosyl Hydrolases; D009244:NAD+ Nucleosidase