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• W2056554325 startingPage "153" @default.
• W2056554325 abstract "Despite the complexity of the subject of protein–alum interactions, a valuable information can be obtained by analyzing the adsorbed and desorbed protein by common physico–chemical methods. In the present work, to approach the adsorption of hepatitis B surface antigen (HBsAg) on alum, the experimental data were supported by complementary analyses of the adsorbed protein by immunoelectron microscopy and the desorbed protein by denaturing size-exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. First, the depletion of HBsAg was investigated. The aspects assessed were the conditions, recovery and chromatographic performance of the desorbed protein. The results obtained strongly suggested the loss of particulate structure of HBsAg after adsorption on alum. This conclusion was further reinforced by direct immunoelectron microscopic visualization of HBsAg in the adsorbed state." @default.
• W2056554325 created "2016-06-24" @default.
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• W2056554325 creator A5041657452 @default.
• W2056554325 creator A5070086089 @default.
• W2056554325 date "1998-12-01" @default.
• W2056554325 modified "2023-09-24" @default.
• W2056554325 title "Evidence for the denaturation of recombinant hepatitis B surface antigen on aluminium hydroxide gel" @default.
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• W2056554325 doi "https://doi.org/10.1016/s0378-4347(98)00425-3" @default.
• W2056554325 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9892077" @default.
• W2056554325 hasPublicationYear "1998" @default.
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