Localization of an arginine-specific mono-ADP-ribosyltransferase in skeletal muscle sarcolemma and transverse tubules.
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.
Klebl
B M
BM
Fakultät für Biologie, Universität Konstanz, Germany.
Matsushita
S
S
Pette
D
D
D036002:ADP Ribose Transferases / Q000032:analysis* / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000818:Animals; D002499:Centrifugation, Density Gradient; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D012508:Sarcolemma / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology
D009124:Muscle Proteins; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases