인간 포미바이러스 인테그라제의 생화학적 특성

• 영문명: Biochemical Characterization of Human Foamy Virus Integrase
• 발행기관: 대한약학회
• 저자명: 강승이(Seung Yi Kang) 오수아(Soo A Oh) 이학성(Hak Sung Lee) 한성태(Sung Tai Han) 서진욱(Jin-Wook Seo) 신차균(Cha-Gyun Shin)
• 간행물 정보: 『약학회지』제48권 제1호 (2004년), 13~19쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2004.02.28

영문 초록

A bacterial expression vector for the human foamy virus (HFV) integrase was constructed and expressed In Escherichia coli. By two-step purification using a nickel-chelated column and a SP-sepharose chromatography, the HFV integrase protein of 43 kDa was purified to near homogeneity, and used to investigate biochemical characteristics of the enzymatic activities, such as endonucleolytic and disintegration activities. 0ligonucleotide substrates were specifically and efficiently cleaved by the purified HFV integrase in the presence of Mn+2, but not in the presence of Mg+2, indicating that the HFV integrase is not able to use Mg+2 as a cofactor. Endonucleolytic reaction was almost completed in 60 min at 37 ℃. In addition, the maximum enzymatic activities were observed at 5 mM Mn+2 in the buffer of which pH was from 7.0 to 9.0. The endonucleolytic activities were dose-dependently blocked in the addition of baicalein or chicolic acid which is a well-known inhibitor of human immunodeficiency virus integrase.

키워드

HFV integrase endonucleolytic disintegration.