Purification and Characterization of the Anti-Plant Viral Protein from Mirabilis jalapa L.
Purification and Characterization of the Anti-Plant Viral Protein from Mirabilis jalapa L.
复制标题
紫茉莉抗植物病毒蛋白的纯化和表征。
DOI：
--
复制
发表时间：
1990
期刊：
影响因子：
--
通讯作者：
S. Kubo
中科院分区：
文献类型：
--
作者：
Y. Takanami;S. Kuwata;T. Ikeda;S. Kubo
从紫茉莉根中分离纯化出一种抗植物病毒机械传播的抗植物病毒蛋白(MAP)，该蛋白经硫酸铵沉淀、CMC型离子交换层析和DEAE-Sepharose型离子交换层析得到纯品。经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法测定，该蛋白含有一条分子量约为24,200的多肽链。其沉降系数为S20，w=2.5。MAP是一种富含赖氨酸的碱性简单蛋白，等电点为9.8，不含糖。MAP的热失活点因Jalapa作为蛋白质来源的特性而不同，提示该分子可能存在一定的变异。粗品中MAP含量可用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法和阳离子交换树脂高效液相色谱法进行定量测定。(1990年1月5日收到)
An anti-plant viral protein (MAP), active against mechanical transmission of plant viruses, was purified to homogeneity from roots of Mirabilis jalapa L. by ammonium sulfate precipitation and ion exchange chromatography with CMand DEAE-Sepharose. The protein consists of a polypeptide chain of an approximate molecular weight of 24,200 estimated by SDS-polyacrylamide gel electrophoresis. Its sedimentation coefficient was S20,w=2.5. MAP was shown to be lysine rich, basic simple protein having isoelectric point of 9.8 and containing no sugar moiety. Thermal inactivation point of MAP varied with the traits of M. jalapa used as the sources of protein preparation, suggesting that there might be some variations in the molecule. MAP content in crude preparations could be quantitatively measured by SDS-polyacrylamide gel electrophoresis and also high performance liquid chromatography using cation exchange resin. (Received January 5, 1990)