Mandersloot J G, Roelofsen B, de Gier J
Biochim Biophys Acta. 1978 Apr 20;508(3):478-85. doi: 10.1016/0005-2736(78)90093-7.
Incubation of rabbit kidney microsomes with pig pancreatic phospholipase A2 produced residual membrane preparations with very low (Na+ + K+)-ATPase activity. The activity could be restored by recombination with lipid vesicles of negatively-charged glycerophospholipids. Vesicles of pure phosphatidylcholine and phosphatidylethanolamine were virtually inactive in this respect, but could reactivate in the presence of cholate. Incubation of the microsomes with a combination of phospholipase C (Bacillus cereus) and spingomyelinase C (Staphylococcus aureus) resulted in 90--95% release of the phospholipids. The residual membrane contained only phosphatidylinositol and still showed 50--100% of the (Na+ + K+)-ATPase activity.
兔肾微粒体与猪胰磷脂酶A2一起温育，产生了具有非常低的（Na⁺ + K⁺）-ATP酶活性的残余膜制剂。该活性可通过与带负电荷的甘油磷脂脂质体重组来恢复。纯磷脂酰胆碱和磷脂酰乙醇胺脂质体在这方面几乎没有活性，但在胆酸盐存在下可重新激活。用磷脂酶C（蜡状芽孢杆菌）和鞘磷脂酶C（金黄色葡萄球菌）的组合温育微粒体，导致90 - 95%的磷脂释放。残余膜仅含有磷脂酰肌醇，并且仍显示出（Na⁺ + K⁺）-ATP酶活性的50 - 100%。
