Tzeng M C, Hseu M J, Yen C H
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, R.O.C.
Biochem Biophys Res Commun. 1989 Dec 15;165(2):689-94. doi: 10.1016/s0006-291x(89)80021-x.
Affinity labeling techniques were used to identify the neuronal membrane molecules involved in the binding of taipoxin, a neurotoxic protein with phospholipase A2 activity. After [125I]taipoxin had bound to synaptosomes from guinea pig brain, treatment with disuccinimidyl suberate resulted in the formation of a predominant radioactive conjugate of 60,000 Da. Notexin and some other PLA2s are weakly inhibitory to this conjugation, while beta-bungarotoxin and some others are not inhibitory. The 60K conjugate was not detected when plasma membranes from several nonneuronal tissues were used. We concluded that a 45,000 Da protein specifically present in neuronal membranes is (a subunit of) the major molecule responsible for taipoxin binding.
亲和标记技术被用于鉴定参与 taipoxin（一种具有磷脂酶 A2 活性的神经毒性蛋白）结合的神经元膜分子。在[125I]taipoxin 与豚鼠脑突触体结合后，用辛二酸二琥珀酰亚胺酯处理导致形成了一种主要的 60,000 Da 放射性共轭物。Notexin 和其他一些磷脂酶 A2 对这种共轭反应有微弱抑制作用，而β-银环蛇毒素和其他一些则没有抑制作用。当使用几种非神经元组织的质膜时，未检测到 60K 共轭物。我们得出结论，神经元膜中特异性存在的一种 45,000 Da 蛋白是负责 taipoxin 结合的主要分子（的一个亚基）。
