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J. Biochem, 1976, Vol. 80, No. 1 167-176
© 1976 Japanese Biochemical Society

research-article

Characterization of the NAD+ Glycohydrolase Associated with the Rat Liver Nuclear Envelope1

Masanori FUKUSHIMA*,2, Hiroto OKAYAMA*, Yohei TAKAHASHI** and Osamu HAYAISHI*

*Department of Medical Chemistry, Kyoto University Faculty of Medicine Sakyo-ku, Kyoto, Kyoto 606
**Department of Pathology, Hamamatsu University School of Medicine Handa-cho, Hamamatsu, Shizuoka 431–31

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 µM), 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.

1 This investigation was supported in part by research grants from the Waksman Foundation of Japan, Inc., the Princess Takamatsu Cancer Research Fund, and by a Grant-in-Aid for Cancer Research from the Ministry of Education, Science and Culture, of Japan

2Present address: Department of Biochemistry, Hamamatsu University School of Medicine, Handacho, Hamamatsu, Shizuoka 431–31.


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