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Localization of an arginine‐specific mono‐ADP‐ribosyltransferase in skeletal muscle sarcolemma and transverse tubules
Author(s) -
Klebl Bert M.,
Matsushita Shigeki,
Pette Dirk
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80586-5
Subject(s) - sarcolemma , skeletal muscle , arginine , membrane , cytoplasm , biochemistry , chemistry , vesicle , biology , amino acid , anatomy
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 [ 32 P]ADP‐ribose‐labeled proteins.