Localization of an arginine‐specific mono‐ADP‐ribosyltransferase in skeletal muscle sarcolemma and transverse tubules

FEBS Letters

Klebl, Bert M.¹  Matsushita, Shigeki¹  Pette, Dirk¹ 

[1] Fakultät für Biologie, Universität Konstanz, Postfach 5560-M641, D-78434 Konstanz, Germany

关键词: Mono-ADP-ribosyltransferase;    Rabbit skeletal muscle;    Sarcolemma;    T-tubule;    C12E9;    polyoxyethylene 9 lauryl ether;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate;    GTP[S];    guanosine 5'|y-thio]triphosphate;    lysoPtdCho;    lysophosphatidylcholine;    mADP-RT;    arginine-speciflc mono-ADP-ribosyltransferase;    PMSF;    phenylmethylsulfonyl fluoride;   

DOI  :  10.1016/0014-5793(94)80586-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The precise localization of a membrane-bound, arginine-specific mono-ADP-ribosyltransferase (mADP-RT) was assessed in rabbit skeletal muscle by studying membrane fractions isolated by successive sucrose density gradient centrifugations. mADP-RT activity was 10-fold enriched in sarcolemmal and T-tubular membranes. The catalytic activity, determined in preparations with mainly right-side-out vesicles, was found to be on the cytoplasmic face. As revealed by SDS-PAGE and autoradiography endogenous mADP-RT activity labeled several proteins in the range between 15 kDa and 250 kDa. T-tubules contained the highest number of [³²P]ADP-ribose-labeled proteins.

【 授权许可】

Unknown