Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process

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	Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process
	Li, Yan ; Bi, Jingxiu ; Zhou, Weibin ; Huang, Yongdong ; Sun, Lijing ; Zeng, An-Ping ; Ma, Guanghui ; Su, Zhiguo
刊名	PROCESS BIOCHEMISTRY
	2007-03-01
卷号	42 期号:3 页码:315-319
关键词	hepatitis B surface antigen (HBsAg) membrane ultrafiltration protein aggregation
ISSN号	1359-5113
其他题名	Process Biochem.
中文摘要	This investigation focused on the structure change of Hepatitis B virus surface antigen (HBsAg) in the process of ultratiltration (UF). Based on the assay of high performance size exclusion chromatography combining with on-line multi-angle laser light scattering (HPSEC-MALLS) and enzyme-linked immunosorbent assay (ELISA), the HBsAg assemblies were found to aggregate into large-size HBsAg aggregation with only about 20% HBsAg activity of the normal HBsAg assembly. The secondary structure of large size HBsAg aggregation was monitored by circular dichroism spectroscopy (CD) and demonstrated that the content of a-helix in HBsAg decreased from 48.2% to 34.4% and the content of gamma-turn increased from 29.6% to 38.7% due to aggregation. The lipid structure of large size HBsAg aggregation was also changed markedly by the assay of infrared spectroscopy (IR) at the wavenumber 1750 cm(-1) which is corresponding to ester acyl. (c) 2006 Elsevier Ltd. All rights reserved.
英文摘要	This investigation focused on the structure change of Hepatitis B virus surface antigen (HBsAg) in the process of ultratiltration (UF). Based on the assay of high performance size exclusion chromatography combining with on-line multi-angle laser light scattering (HPSEC-MALLS) and enzyme-linked immunosorbent assay (ELISA), the HBsAg assemblies were found to aggregate into large-size HBsAg aggregation with only about 20% HBsAg activity of the normal HBsAg assembly. The secondary structure of large size HBsAg aggregation was monitored by circular dichroism spectroscopy (CD) and demonstrated that the content of a-helix in HBsAg decreased from 48.2% to 34.4% and the content of gamma-turn increased from 29.6% to 38.7% due to aggregation. The lipid structure of large size HBsAg aggregation was also changed markedly by the assay of infrared spectroscopy (IR) at the wavenumber 1750 cm(-1) which is corresponding to ester acyl. (c) 2006 Elsevier Ltd. All rights reserved.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Technology
类目[WOS]	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical
研究领域[WOS]	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering
关键词[WOS]	HANSENULA-POLYMORPHA ; PROTEIN ; PARTICLES ; CELLS ; PURIFICATION
收录类别	SCI
原文出处	://WOS:000245021300003
语种	英语
WOS记录号	WOS:000245021300003
公开日期	2013-10-15
内容类型	期刊论文
版本	出版稿
源URL	[http://ir.ipe.ac.cn/handle/122111/3377]
专题	过程工程研究所_研究所（批量导入）
作者单位	1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Tech Univ Hamburg, Inst Bioproc & Biosyst Engn, D-21073 Hamburg, Germany
推荐引用方式 GB/T 7714	Li, Yan,Bi, Jingxiu,Zhou, Weibin,et al. Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process[J]. PROCESS BIOCHEMISTRY,2007,42(3):315-319.
APA	Li, Yan.,Bi, Jingxiu.,Zhou, Weibin.,Huang, Yongdong.,Sun, Lijing.,...&Su, Zhiguo.(2007).Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process.PROCESS BIOCHEMISTRY,42(3),315-319.
MLA	Li, Yan,et al."Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process".PROCESS BIOCHEMISTRY 42.3(2007):315-319.