| Object: In order to provide a foundation for ginseng's study of structure and function, we constituted a simple and efficient technology of purification, and studied the physical, chemical and heated characters.Method: The aggregate proteins were purified by means of salt solution extraction, (NH4)2SO4 precipitation, ultrafiltration, affinity chromatography, iron exchange chromatography and hydrophobic interaction chromatography; then the aggregate protein and their purities were identified by SDS-polyacrylamide gels electrophoresis and Gel Filtration chromatography.Result: 1. Five kinds of proteins were purified from ginseng, and the corresponding protocol of purification were established.2. The purification of proteins were attained to the standard of SDS-PAGE and HPLC.3. The percentage of receival in ginseng was above 80% except for GP1 and GP2.4. The ginseng proteins called GP1,GP2,GP3,GP5 were all single-subunit proteins, and their molecular weights were 25kDa,65kDa,15kDa and 8kDa, while the GP4 was glycoprotein containing two subunits whose molecular were 29kDa and 27kDa.5. Among the purified five kinds of proteins, GP1 is similar ribonuclease, GP3 is chitinase-like protein, GP4 is ginseng ribonuclease; two kinds of ginseng protein called GP2 and GP5 were all reported for the first time.6. Upon further heating temperature, the soluble gingseng proteins were associated to form insoluble aggregates and(or) dissociated to form subunits. Upon the time of heating, the proteins were associated to form big and soluble aggregates at 50℃.Conclusion: Aiming at the important Chinese traditional medicine—ginseng, we studied the high concentration of protein from it. This research adopted advanced biological technology to isolate and purify five kinds of proteins, and then we studied the heated characters of ginseng, and the consequent data were obtained. Two of the purities were reported for the first time. Those results would provide a foundation for the farther research. |
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