Zaheer A, Iyer S S, Braganca B M
Cancer Biochem Biophys. 1979;3(3):123-7.
Inactivation of (Na+ + K+)-ATPase of Yoshida sarcoma cells and beef brain microsomes by phospholipase A2 and a cytotoxin P6 from snake venom has been examined in relation to their activity to degrade phospholipids. Cytotoxin P6 which was most basic and devoid of phospholipase activity was most effective in inhibiting the (Na+ + K+)-ATPase of Yoshida sarcoma cells. Phospholipase A2 from Naja naja which was most active in degrading phospholipids was least effective in inhibiting (Na+ + K+)-ATPase in Yoshida sarcoma cells or in beef brain microsomes. Addition of trace amounts of cytotoxin P6 to the phospholipase considerably enhanced the inactivation of (Na+ + K+)-ATPase. The evidence suggests that the charge of the inhibitor protein and its specific structure play an important role in the inactivation of (Na+ + K+)-ATPase.
研究了磷脂酶A2和一种来自蛇毒的细胞毒素P6对吉田肉瘤细胞和牛脑微粒体中(Na+ + K+)-ATP酶的失活作用,并将其与它们降解磷脂的活性相关联。细胞毒素P6碱性最强且无磷脂酶活性,对抑制吉田肉瘤细胞的(Na+ + K+)-ATP酶最为有效。眼镜蛇的磷脂酶A2在降解磷脂方面活性最高,但在抑制吉田肉瘤细胞或牛脑微粒体中的(Na+ + K+)-ATP酶方面效果最差。向磷脂酶中添加微量细胞毒素P6可显著增强(Na+ + K+)-ATP酶的失活作用。证据表明,抑制蛋白的电荷及其特定结构在(Na+ + K+)-ATP酶的失活中起重要作用。