黑豆盐溶球蛋白的研究

Study of salt-soluble globulin from black soya (Semen glycine)

对经凝胶过滤后的黑豆盐溶球蛋白进行Native-PAGE及双向SDS-PAGE电泳分析,结果表明黑豆7S球蛋白是由3个以非共价键相结合的亚基 MW:84.7kD,72.6kD和49.2kD 连接而成;黑豆11S球蛋白中则含有以共价键相结合的亚基,同时也可能存在非共价键结合的亚基.其在还原条件下,可分解出5个肽链 MW:38.4kD,35.4kD,34.5kD,21kD和20.6kD ,且在电泳图片上明显分为两个区域.

This paper presents the analysis of saltsoluble globulin from black soya by NativePAGE and SDSPAGE electrophoresis after gel filtration.The purified 7S globulin was found to be composed of three noncovalently linked subunits namely:84.7 kD,72.6 kD and 49.2 kD.From the resultsof twodimensiton electrophoresis in this study,the 11S globulin was found to be composed of both covalently and noncovalently linked subunits,and in the condition of reducing,it was dissociated into five subunits namely:38.4 kD,35.4 kD,34.5 kD,21 kD and 20.6 kD.All those subunits from 11S globulin are located within two narrow molecular ranges and was believed to correspond to basic and acid subunits,respectively.