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

Paper ID Volume ID Publish Year Pages File Format Full-Text
36126 45122 2007 5 PDF Available
Title
Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process
Abstract

This investigation focused on the structure change of Hepatitis B virus surface antigen (HBsAg) in the process of ultrafiltration (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 α-helix in HBsAg decreased from 48.2% to 34.4% and the content of γ-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.

Keywords
Hepatitis B surface antigen (HBsAg); Membrane ultrafiltration; Protein aggregation
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Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 3, March 2007, Pages 315–319
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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Any Questions? feel free to contact us