Expression and Purification of Herpes Simplex Virus Type 1 Protease
Journal of the Korean Society of Virology
;
: 175-182, 1999.
Article
in Korean
| WPRIM
| ID: wpr-27129
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Base Sequence
/
Chromatography, High Pressure Liquid
/
Chromatography, Liquid
/
Amino Acid Sequence
/
Clone Cells
/
Simplexvirus
/
Herpesvirus 1, Human
/
Catalytic Domain
/
DNA Packaging
/
Drug Therapy
Language:
Korean
Journal:
Journal of the Korean Society of Virology
Year:
1999
Type:
Article
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