Dean W L, Tanford C
J Biol Chem. 1977 May 25;252(10):3551-3.
The Ca2+-ATPase of sarcoplasmic reticulum can be reversibly delipidated by precipitation with polyethyleneglycol in the presence of deoxycholate and glycerol to as low as 4 mol of phospholipid/mol of enzyme polypeptide and can then be reactivated to 90% of its original ATPase activity by the addition of phosphatidylcholine. Furthermore, the preparation exhibits nearly the same activity if the nonionic detergent dodecyl octaoxyethyleneglycol monoether is substituted for the added phospholipid. The delipidated ATPase is soluble in the detergent and retains activity for several days. This is the first report of the Ca2+-ATPase retaining high activity with less than about 30 mol of phospholipid bound per mol of polypeptide.
肌质网的Ca2 + -ATP酶在脱氧胆酸盐和甘油存在的情况下，可通过聚乙二醇沉淀进行可逆性脱脂，使磷脂与酶多肽的摩尔比低至4摩尔/摩尔，然后通过添加磷脂酰胆碱可将其重新激活至原始ATP酶活性的90%。此外，如果用非离子洗涤剂十二烷基八氧乙烯乙二醇单醚替代添加的磷脂，该制剂表现出几乎相同的活性。脱脂的ATP酶可溶于洗涤剂中，并保持活性数天。这是关于Ca2 + -ATP酶在每摩尔多肽结合少于约30摩尔磷脂的情况下仍保持高活性的首次报道。
