Madeira V M
Biochim Biophys Acta. 1977 Feb 4;464(3):583-8. doi: 10.1016/0005-2736(77)90032-3.
Sarcoplasmic reticulum membranes with high content of Ca2+ -ATPase (80% of total protein) were dissolved in a non ionic medium and were submitted to isoelectric focusing in polyacrylamide gels. The membrane protein was resolved into six main bands whose isoelectric points range from 6 to 5. The mol. wt. of these peptides is about 100 000 as estimated by second dimension electrophoresis in sodium dodecyl sulfate-polyacrylamide system. The electrophoretic behaviour of the purified ATPase enzyme is similar to that of crude membranes.
含有高含量钙-ATP酶（占总蛋白的80%）的肌浆网膜溶解于非离子介质中，并在聚丙烯酰胺凝胶中进行等电聚焦。膜蛋白被分离成六条主要条带，其等电点范围为6至5。在十二烷基硫酸钠-聚丙烯酰胺系统中通过二维电泳估计，这些肽的分子量约为100000。纯化的ATP酶的电泳行为与粗膜相似。
