Potter L T, Hanchett-Valentine H, Liang J S, Max S I, Purkerson S L, Silberberg H A, Strauss W L
Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, FL.
Life Sci. 1993;52(5-6):433-40. doi: 10.1016/0024-3205(93)90299-i.
The venom of the Eastern green mamba from Africa, Dendroaspis angusticeps, contains a number of toxins which block the binding of 3H-antagonists to genetically-defined m1 and m4 muscarinic acetylcholine receptors. Most of the anti-muscarinic activity of the venom is due to the presence of a newly-isolated toxin, "m1-toxin", which has 64 amino acids and a molecular mass of 7361 Daltons. At present m1-toxin is the only ligand which is known to be capable of fully blocking m1 receptors without affecting m2-m5 receptors. It binds very rapidly, specifically and pseudoirreversibly to the extracellular face of m1 receptors on cells, in membranes or in solution, whether or not the primary receptor site is occupied by an antagonist. Bound toxin can either prevent the binding and action of agonists or antagonists, or prevent the dissociation of antagonists. The toxin is useful for identifying m1 receptors during anatomical and functional studies, for recognizing and stabilizing receptor complexes, and for occluding m1 receptors so that other receptors are more readily studied.
非洲东部绿曼巴蛇(Dendroaspis angusticeps)的毒液含有多种毒素,这些毒素会阻断3H拮抗剂与基因定义的m1和m4毒蕈碱型乙酰胆碱受体的结合。毒液的大部分抗毒蕈碱活性归因于一种新分离出的毒素“m1毒素”,它含有64个氨基酸,分子量为7361道尔顿。目前,m1毒素是已知唯一能够完全阻断m1受体而不影响m2 - m5受体的配体。它能非常迅速、特异性且假不可逆地结合细胞、膜或溶液中m1受体的细胞外表面,无论初级受体位点是否被拮抗剂占据。结合的毒素既可以阻止激动剂或拮抗剂的结合与作用,也可以阻止拮抗剂的解离。该毒素在解剖学和功能研究中有助于识别m1受体,用于识别和稳定受体复合物,以及封闭m1受体,从而更便于研究其他受体。