Auguste P, Hugues M, Borsotto M, Thibault J, Romey G, Coppola T, Lazdunski M
Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France.
Brain Res. 1992 Dec 25;599(2):230-6. doi: 10.1016/0006-8993(92)90396-q.
This work describes the partial purification of a heat-stable peptide which has the same properties as the scorpion toxin, scyllatoxin, a specific blocker of one class of Ca(2+)-activated K+ channels: (i) it competes with [125I]apamin for binding to the same site, (ii) like apamin and scyllatoxin, it blocks the after-potential hyperpolarization in skeletal muscle cells in culture, (iii) like apamin and scyllatoxin, it contracts guinea-pig taenia coli relaxed by epinephrine, (iv) it cross-reacts with antibodies raised against scyllatoxin but not with antibodies raised against apamin.
这项工作描述了一种热稳定肽的部分纯化过程，该肽具有与蝎毒素、岩藻毒素相同的特性，岩藻毒素是一类钙激活钾通道的特异性阻滞剂：（i）它与[125I]蜂毒明肽竞争结合同一位点；（ii）与蜂毒明肽和岩藻毒素一样，它能阻断培养的骨骼肌细胞中的后超极化电位；（iii）与蜂毒明肽和岩藻毒素一样，它能使肾上腺素松弛的豚鼠结肠带收缩；（iv）它与抗岩藻毒素产生的抗体发生交叉反应，但不与抗蜂毒明肽产生的抗体发生交叉反应。
