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- W2026339990 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." @default.
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- W2026339990 date "2007-03-01" @default.
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- W2026339990 title "Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process" @default.
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- W2026339990 doi "https://doi.org/10.1016/j.procbio.2006.08.016" @default.
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