Ginseng root saponins ( GRS ) was extracted from native ginseng.The dosage used was calculated according to the content of saponins.Immunosuppression in mice was induced in 15 days after implar- ting Ehrlich ascites carcinoma (EAC) subcutaneously in armpit, and in 5-11 days after implanting EAC into peritoneal cavity. GRS administered orally 50mg/kg- for 8 days did not prevent the atrophy of the thymus in tumor-bearing mice but rather aggravated it. GRS administered orally 50mg/kg for 14 days partially restored the suppressed phagocytosis of peritoneal macrophages in tumor-bearing mice. GRS administered orally 50mg/kg for 6 days somewhat restored the suppression of hemolysin formation in tumor-bearing mice 5 days after implanting EAC, But GRS given in the same route and dosage for 9 days, showed no effect on the suppression of hemolysin formation. GRS administered orally 50mg/kg for 10 days partially restored the suppression of delayed hypersensitive reaction in tumor-bearing mice.

Objective To construct a CaME141G fusion protein-expressing plasmid,and to express,purify,and identify the activity of the recombinant protein. Methods The 141st site of the wild type CaM,E (GAG),was mutated to G (GGG),using site-specific mutagenesis technology. Escherichia coli BL-21 was transformed with the mutant plasmid. The GST-CaME141G fusion protein was mass-cultured and induced for expression. Subsequently,the GST-CaME141G fusion protein was purified using GS-4B beads. PreScission protease was applied to remove the GST,the Bradford method used to determine the concentration of purified protein,and SDS-PAGE used to detect its relative molecular weight and purity. The GST pull-down assay was used to study the protein's biological activity. Results The CaME141G protein was successfully purified at a high concentration and purity. The protein could interact with PreIQ protein fragments from the myocardial CaV1. 2 calcium channel C terminal,in a CaME141G concentration-dependent manner. Therefore,CaME141G has the ability to bind with the CaV1. 2 calcium channel. Conclusion This study successfully constructed a CaME141G fusion protein-expressing plasmid and purified the CaME141G protein. This lays a foundation for regulating the function of CaM mutations in the myocardial CaV1. 2 calcium channel,and for the study of its relationship with diseases of the cardiovascular system.