Alzahaby M, Harvey A L, Young L C, Faure G, Rowan E G
Department of Physiology and Pharmacology, University of Strathclyde, Glasgow, UK.
Toxicon. 1998 Apr;36(4):601-7. doi: 10.1016/s0041-0101(97)00108-6.
A protein that inhibits the re-uptake of 5-hydroxytryptamine into rat brain synaptosomes was isolated from the venom of the Sahara sand viper (Cerastes vipera) by gel filtration and reverse phase chromatography. It has a molecular weight of 13,739 Da and an IC50 of about 50 nM for blocking uptake of 3H-5-HT into rat brain synaptosomes. It also augmented the responses to 5-HT in a smooth muscle preparation. It has phospholipase A2 activity, but it has no lytic activity as measured by its inability to release lactate dehydrogenase from rat brain synaptosomes. Determination of the N-terminal sequence revealed a similarity with a phospholipase A2 previously isolated from Cerastes cerastes venom.
通过凝胶过滤和反相色谱法,从撒哈拉沙漠角蝰(Cerastes vipera)的毒液中分离出一种抑制5-羟色胺再摄取到大鼠脑突触体中的蛋白质。它的分子量为13739道尔顿,在阻断3H-5-羟色胺摄取到大鼠脑突触体中的IC50约为50纳摩尔。它还增强了平滑肌制剂对5-羟色胺的反应。它具有磷脂酶A2活性,但通过其无法从大鼠脑突触体中释放乳酸脱氢酶来衡量,它没有裂解活性。N端序列的测定显示与先前从角蝰毒液中分离出的一种磷脂酶A2相似。