2007
DOI: 10.1016/j.procbio.2006.08.016
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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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Cited by 25 publications
(10 citation statements)
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“…Note that the protruded surface features of the HBsAg particles are much better defined after KSCN-induced oxidative maturation with more interchain cross-linking via disulfide bonds (Wampler et al 1985). Size characterization and monitoring of aggregation during processing steps could be monitored by CD and HPSEC-MALLS (Li et al 2007).…”
Section: Modern Characterization Methodsmentioning
confidence: 99%
“…Note that the protruded surface features of the HBsAg particles are much better defined after KSCN-induced oxidative maturation with more interchain cross-linking via disulfide bonds (Wampler et al 1985). Size characterization and monitoring of aggregation during processing steps could be monitored by CD and HPSEC-MALLS (Li et al 2007).…”
Section: Modern Characterization Methodsmentioning
confidence: 99%
“…Although various SLPPs have been successfully purified with chromatography and membrane‐based separation techniques, there are many reports on denaturation or significant loss of SLPPs during these two methods [15]. For example, in the purification of hepatitis B surface antigen (HBs VLPs), a single ion exchange chromatography (IEC) or ultrafiltration step would lead to 20–40% loss in the total antigen recovery [16, 17], accompanied with the VLPs aggregation and dissociation. These failures expose the fact that we still do not fully understand the denaturation mechanisms and how to stabilize SLPPs during purification.…”
Section: Challenges In Manufacturing Of Slppsmentioning
confidence: 99%
“…The group has successfully refolded some proteins, such as Hepatitis B virus surface antigen (HBsAg), Consensus interferon (C-IFN), etc. [74,75].…”
Section: Renaturation and Modification Of Proteinsmentioning
confidence: 99%