Characterization of sarcolemma from rabbit skeletal muscle.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis reveals in the rabbit skeletal muscle sarcolemma the presence of four major protein bands corresponding to molecular weight 216,000, 110,000, 44,000, 15,000, and smaller amounts of 148,000, 78,000, 68,000, 37,000, 27,000 proteins. (Na+-K+)-ATPase isolated from rabbit skeletal muscle contains 102,000, 44,000, and 32,000 protein bands. Sarcolemma is resistant to the solubilizing effect of Triton X-100, Lubrol, and deoxycholate. Sarcolemmal proteins, especially sodium-potassium-ATPase, are sensitive to digestion with trypsin.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D003840:Deoxycholic Acid; D008055:Lipids / Q000032:analysis; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D009132:Muscles / Q000032:analysis* / Q000201:enzymology; D011092:Polyethylene Glycols; D011817:Rabbits; D012508:Sarcolemma / Q000032:analysis* / Q000201:enzymology / Q000648:ultrastructure; D013501:Surface-Active Agents
D002241:Carbohydrates; D008055:Lipids; D009124:Muscle Proteins; D013501:Surface-Active Agents; D003840:Deoxycholic Acid; D011092:Polyethylene Glycols; D000251:Adenosine Triphosphatases