Structural membrane proteins and loosely associated proteins of the sarcoplasmic reticulum.
The protein composition of sarcoplasmic-reticulum vesicles, either unpurified or after fractionation on sucrose gradients, and with or without previous osmotic shock and sonication, was investigated by electrophoresis in acid polyacrylamide gels. The pattern of release of loosely bound proteins is discussed with respect to their localization in the interior of the vesicles.
D000251:Adenosine Triphosphatases; D000255:Adenosine Triphosphate; D000818:Animals; D002499:Centrifugation, Density Gradient; D003579:Cytochrome Reductases / Q000032:analysis; D003574:Cytochrome c Group / Q000378:metabolism; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D008566:Membranes / Q000032:analysis; D008722:Methods; D009124:Muscle Proteins / Q000032:analysis; D009243:NAD / Q000378:metabolism; D009996:Osmotic Fragility; D010761:Phosphorus Radioisotopes; D011485:Protein Binding; D011506:Proteins / Q000032:analysis*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000032:analysis*; D013386:Succinates / Q000378:metabolism; D014461:Ultracentrifugation; D014465:Ultrasonics
D003574:Cytochrome c Group; D009124:Muscle Proteins; D010761:Phosphorus Radioisotopes; D011506:Proteins; D013386:Succinates; D009243:NAD; D000255:Adenosine Triphosphate; D003579:Cytochrome Reductases; D000251:Adenosine Triphosphatases