Kemparaju K, Prasad B N, Gowda V T
Department of Studies in Biochemistry, University of Mysore, Manasa Gangothri, India.
Toxicon. 1994 Oct;32(10):1187-96. doi: 10.1016/0041-0101(94)90348-4.
A major basic phospholipase A2 was purified from the Indian saw-scaled viper (Echis carinatus) venom by the combination of column chromatography and electrophoresis. The purified phospholipase A2 (EC-IV-PLA2) has a mol. wt of 14,000 by SDS-PAGE. It is a basic protein with a pI value between 7.2 and 7.6, and has a fluorescence emission maxima at 340 nm. It induces neurotoxicity and oedema in mice with an i.p. LD50 of 5 mg/kg body weight. It is devoid of direct haemolytic, myotoxic, cytotoxic and anticoagulant activities. Rabbit polyclonal antibodies prepared against EC-IV-PLA2 inhibited the in vitro enzymatic activity dose dependently, but did not neutralize the toxic effects of EC-IV-PLA2 in experimental animals.
通过柱色谱和电泳相结合的方法，从印度锯鳞蝰蛇（锯鳞蝰）毒液中纯化出一种主要的碱性磷脂酶A2。经SDS-PAGE分析，纯化后的磷脂酶A2（EC-IV-PLA2）分子量为14,000。它是一种碱性蛋白，pI值在7.2至7.6之间，在340 nm处有最大荧光发射峰。腹腔注射时，它对小鼠具有神经毒性并可导致水肿，半数致死剂量（LD50）为5 mg/kg体重。它没有直接的溶血、肌毒、细胞毒和抗凝活性。针对EC-IV-PLA2制备的兔多克隆抗体可剂量依赖性地抑制其体外酶活性，但不能中和EC-IV-PLA2在实验动物中的毒性作用。
