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Arch Biochem Biophys ; 237(1): 43-54, 1985 Feb 15.
Article in English | MEDLINE | ID: mdl-3155929

ABSTRACT

Vesiculated fragments of chicken skeletal muscle transverse tubule (TT) membranes were analyzed for their content of loosely associated and integral membrane proteins. Of particular interest was the identification of the magnesium-stimulated ATPase (Mg-ATPase), which is characteristically located in native isolated TT vesicles of chicken skeletal muscle [R. A. Sabbadini and V. R. Okamoto (1983) Arch. Biochem. Biophys. 223, 107-119]. A number of the proteins found in vesicular TT preparations were found to be extractable by a mild Triton-X100 treatment and were identified as aldolase, enolase, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and pyruvate kinase. Approximately 60% of TT-associated protein was extracted with Triton, resulting in a twofold enrichment of the Mg-ATPase. Concommitantly, one core integral membrane protein possessing a Mr of 102,000 was enriched, suggesting that it is responsible for the Mg-ATPase activity present in chicken skeletal muscle TT membranes.


Subject(s)
Adenosine Triphosphatases/isolation & purification , Membrane Proteins/isolation & purification , Microtubule Proteins/isolation & purification , Animals , Ca(2+) Mg(2+)-ATPase , Chemical Phenomena , Chemistry , Chickens , Electrophoresis, Polyacrylamide Gel , Fructose-Bisphosphate Aldolase/isolation & purification , Glyceraldehyde-3-Phosphate Dehydrogenases/isolation & purification , Hydrogen-Ion Concentration , Intracellular Membranes/enzymology , Molecular Weight , Sarcolemma/enzymology , Sarcoplasmic Reticulum/enzymology
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