Schengrund C L, DasGupta B R, Ringler N J
Department of Biological Chemistry, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.
Neurosci Lett. 1993 Aug 20;158(2):159-62. doi: 10.1016/0304-3940(93)90253-h.
Tetanus toxin (TTx) and botulinum toxin serotype A (BTxA), preincubated with trisialoganglioside GT1b, adhere to proteins present on blots of bovine synaptosomal proteins. Differential solubilization and ammonium sulfate fractionation provided material enriched in two proteins that appeared to be adhered to most strongly by the labeled neurotoxins. After excision of the appropriate bands from blots of electrophoretically separated proteins, N-terminal amino acid sequence analysis permitted identification of the proteins as synapsins Ia and Ib. Comparison of the effectiveness of different gangliosides at enhancing adherence of the neurotoxins to blots of synapsins Ia and Ib indicated that GD3 was most effective.
破伤风毒素(TTx)和A型肉毒杆菌毒素(BTxA)与三唾液酸神经节苷脂GT1b预孵育后,会黏附于牛突触体蛋白印迹上的蛋白质。差异溶解和硫酸铵分级分离得到了富含两种蛋白质的物质,这两种蛋白质似乎与标记的神经毒素结合最为紧密。从电泳分离的蛋白质印迹上切下合适的条带后,通过N端氨基酸序列分析确定这两种蛋白质为突触素Ia和Ib。比较不同神经节苷脂增强神经毒素与突触素Ia和Ib印迹结合的效果表明,GD3最为有效。