1.Effects of Yinzhihuang Oral Solution on Immunological Liver Injury
Jun QIU ; Rongfen HE ; Liang GAO
China Pharmacy 2007;0(27):-
OBJECTIVE:To investigate the effects of Yinzhihuang oral solution on immunological liver injury (ILI). METHODS:Male mice were randomly divided into blank group (normal saline), model group (normal saline), bifendate group(150 mg?kg-1),high dosage group (Yinzhihuang oral solution 30 mL?kg-1), medium dosage group (Yinzhihuang oral solution 20 mL?kg-1) and low dosage group (Yinzhihuang oral solution 10 mL?kg-1). All rats were given medicine via i.g. gtt for 10 days. ILI model was induced by intravenous injection of bacillus calmette-guerin vaccine (BCG) and lipopolysaccharides (LPS). The content of IL-6 and TNF-? were detected by ELISA. The levels of ALT, AST, MDA and SOD were detected by spectrophotometer. RESULTS:Compared with model group, the level of ALT, AST, MDA, IL-6 and TNF-? were decreased significantly in high dosage, medium dose and low dosage groups (P
2.Application of Multimedia Technology to Optimize Biochemistry Teaching
Gang HUANG ; Fengtian HE ; Rongfen LI ; Jiahe PENG
Chinese Journal of Medical Education Research 2005;0(06):-
Through introducing and summarizing the application of multimedia technology in the process of biochemistry teaching,the article discusses the contribution of multimedia technology in teaching method,teaching organization,teaching content and so on and points out the importance of multimedia technology in biochemistry teaching.
3.Preparation and functional identification of human high mobility group box-1 protein
Xiaoru XING ; Fengtian HE ; Zhaohui YANG ; Rongfen LI ; Yingru ZHENG ; Huiguang GAO ; Song LI ; Yan ZHANG ; Li ZHANG
Journal of Third Military Medical University 2003;0(19):-
Objective To clone the cDNA encoding human HMGB1, express it in E. coli, and identify its biological activity. Methods Human HMGB1 cDNA was amplified by RT-PCR and cloned into vector pUC19. After sequence analysis, the cDNA was ligated into prokaryotic expression vector pQE-80L and induced by IPTG to express HMGB1. The protein was purified with Ni~(2+)-NTA chromatography and polymyxin B affinity column. To identify the function of purified protein, the product was co-cultured with THP1 cells. Results Recombinant expression plasmid pQE-80L/HMGB1 was constructed successfully. After purification, the protein purity reached 96%. The recombinant HMGB1 stimulated THP1 to secrete TNF-? . Conclusion The highly purified HMGB1 was obtained successfully, which showed biological activity. These results lay the foundation for further research on the function of human HMGB1.