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Herpes Simplex Virus Type 1 Protease의 발현 및 분리 정제
배판기(Pan Gee Bae),팽진욱(Jin Wook Paeng),김지현(Ji Hyun Kim),김해수(Hae Soo Kim),백상기(Sang Gee Baek),정인권(In Gwon Jung),이종교(Jong Gyo Lee) 대한바이러스학회 1999 Journal of Bacteriology and Virology Vol.29 No.3
An attractive target for anti-herpes chemotherapy is the herpes simplex virus 1 (HSV-1) protease encoded by the UL26 gene. HSV-1 protease is essential for DNA packaging and virus maturation. To perform high throughput for potent inhibitors, the efficient production of larger amounts of highly purified enzyme and protease activity assay method must be established. In this report, expression in E, coli and purification of the protease gene of HSV-1 strain F was investigated. The protease gene was cloned pET28, and the nucleotide sequence of protease catalytic domain of HSV-1 compared strain F with other strains (KOS and CL101). In these results the F strain was different in base sequence. However, the amino acid sequence was identifical. The HSV-1 protease was purified with His-tagged affinity column. The analysis of HSV-1 protease activity was performed by high performance liquid chromatography.