The Journal of Korean Society of Virology (대한바이러스학회지)

The Korean Society of Virology (대한바이러스학회)
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Expression and Purification of Herpes Simplex Virus Type 1 Protease

Herpes Simplex Virus Type 1 Protease의 발현 및 분리 정제

  • Bae, Pan-Kee (Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology) ;
  • Paeng, Jin-Wook (Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology) ;
  • Kim, Jee-Hyun (Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology) ;
  • Kim, Hae-Soo (Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology) ;
  • Paik, Sang-Gi (Department of Biology, Chungnam National University) ;
  • Chung, In-Kwon (Department of Biology, Yonsei University) ;
  • Lee, Chong-Kyo (Pharmaceutical Screening Center, Korea Research Institute of Chemical Technology)
  • 배판기 (한국화학연구소 의약활성연구실) ;
  • 팽진욱 (한국화학연구소 의약활성연구실) ;
  • 김지현 (한국화학연구소 의약활성연구실) ;
  • 김해수 (한국화학연구소 의약활성연구실) ;
  • 백상기 (충남대학교 생물학과) ;
  • 정인권 (연세대학교 생물학과) ;
  • 이종교 (한국화학연구소 의약활성연구실)
  • Published : 1999.09.30
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Abstract

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.

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