中文摘要：

Muncl3-1 是 synaptic 泡 releasingmachinery.Three 老鼠 Muncl3-1 构造的一个必要部件讲道理地基于相同和功能被设计，在上在 Escherichia 关口 i 表示了，并且比房间文化的 2 亩 g/ml 高与最后的收益净化了到同质。净化的 Muncl3-1 recombinant 蛋白质有不同 oligomericstates， monodispersity 和同质性质。他们的第二等的结构的内容被圆形的二色性方法分析，并且这些 recombinant 蛋白质的沉积系数被 Munc 13-1was 的长螺旋状的像捆的拓扑学首先由我们的数据的分析揭示了的分析 ultracentrifugation.The 测量。另外，这些净化的 recombinant 蛋白质在 mammalianMunc 上为进一步生物化学、生物物理、结构的研究提供理想的开始的材料 13 蛋白质。

英文摘要：

Munc13-1 is an essential component of synaptic vesicle releasing machinery. Three rat Munc 13-1 constructs were rationally designed based on homology and function, overexpressed in Escherichia coli, and purified to homogeneity with a final yield higher than 2 ~tg/ml of cell culture. The purified Munc 13-1 recombinant proteins had distinct oligomeric states, monodispersity and homogeneity properties. Their secondary structural contents were analyzed by the circular dichroism method, and the sedimentation coefficients of these recombinant proteins were measured by analytical ultracentrifugation. The long helical bundle-like topology of Munc 13-1 was first revealed by analysis of our data. In addition, these purified recombinant proteins provide ideal starting materials for further biochemical, biophysical, and structural studies on mammalian Munc 13 proteins.