This study was intended to establish a method of purification of HPV16 L1 protein expressed in a prokaryotic system and to obtain the purified protein. The prokaryotic expression vector pGEX-4T-1-HPV16 L1 was constructed and transformed into E. coli BL21 cell, and induced by 1 mM IPTG to express HPV16L1 protein. The inclusion bodies were isolated and solubilized with 8 M urea. After the urea was removed by gradual dialysis, the denatured L1 protein were renatured and then were purified by affinity chromatography. The results showed that HPV16L1 protein formed inclusion bodies in bacterial expression system, suggesting that this assay can be used to purify HPV16L1 protein and hence provide a basis for studying the applications of HPV16 L1 protein.
[Expression and purification of human papillomavirus type16 L1 protein in a prokaryotic expression system] Publishing Authors By Initials
[Expression and purification of human papillomavirus type16 L1 protein in a prokaryotic expression system] Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Sheng wu yi xue gong cheng xue za zhi = Journal of
VOLUME: 19
Page Numbers: 280-3
Journal Abbreviation:
ISSN: 1001-5515
DAY: 12
MONTH: Jun
YEAR: 2002
[Expression and purification of human papillomavirus type16 L1 protein in a prokaryotic expression system] Information
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LANGUAGE: chi
NlmUniqueID: 9426398
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Grant and Affiliation Information for [Expression and purification of human papillomavirus type16 L1 protein in a prokaryotic expression system]
AFFILIATION: Department of Microbiology, Harbin Medical University, Harbin 150086.
Country: China
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MEDLINETA: Sheng Wu Yi Xue Gong Cheng Xue
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