Garret C, Cottin P, Dufourcq J, Ducastaing A
Dépt Alimentation et Nutrition, Université de Bordeaux I, Talence, France.
FEBS Lett. 1988 Jan 25;227(2):209-14. doi: 10.1016/0014-5793(88)80900-1.
Possible interactions between calpain II and phospholipids such as phosphatidylinositol, phosphatidylserine and phosphatidylcholine were studied using fluorescence and gel filtration techniques. Changes in fluorescence intensity of purified calpain II show that the enzyme strongly interacts with phosphatidylinositol and phosphatidylserine and to a lesser extent with phosphatidylcholine. These results are corroborated by the gel filtration technique which permits the isolation of the enzyme phospholipid complex. Association between calpain II and various phospholipid vesicles can occur in the absence of calcium. Such binding occurs without any observable change of the molecular mass of the two subunits on SDS-polyacrylamide gel electrophoresis.
利用荧光和凝胶过滤技术研究了钙蛋白酶II与磷脂（如磷脂酰肌醇、磷脂酰丝氨酸和磷脂酰胆碱）之间可能的相互作用。纯化的钙蛋白酶II荧光强度的变化表明，该酶与磷脂酰肌醇和磷脂酰丝氨酸强烈相互作用，与磷脂酰胆碱的相互作用较弱。凝胶过滤技术证实了这些结果，该技术能够分离酶-磷脂复合物。在没有钙的情况下，钙蛋白酶II与各种磷脂囊泡之间可能会发生结合。这种结合在SDS-聚丙烯酰胺凝胶电泳上没有观察到两个亚基分子量的任何变化。
