| Literature DB >> 2783110 |
Y Tanaka1, K Yoshihara, T Kamiya.
Abstract
The acceptors of endogenously catalyzed monoADP-ribosylation in the cell free extract from rat skeletal muscle was searched. The main acceptor proteins in particulate were electrophoretically 52, 80, 100, and greater than 200 kDa proteins in the presence of SDS, while that in cytosol were 36 and 39 kDa proteins. Although no ADP-ribosylation was observed in particulate when the substrate NAD+ was replaced by ADP-ribose, the same ADP-ribose adducts were also formed with higher degree in cytosol. These results indicate that an enzymic and nonenzymic monoADP-ribosylation occur separately in cytosol and particulate. One acceptor, 36 kDa protein, appears to be glyceraldehyde-3-phosphate dehydrogenase.Entities:
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Year: 1989 PMID： 2783110 DOI： 10.1016/0006-291x(89)92329-2
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575