Kanzo
Online ISSN : 1881-3593
Print ISSN : 0451-4203
ISSN-L : 0451-4203
Roles of polymerized human senlm albumin for mechanism of attachment of HB virus against human liver cells
Takao TSUJI
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Keywords: albumin receptor
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1983 Volume 24 Issue 3 Pages 271-277

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Abstract
For detection and characterization of the binding-sites on HB surface antigen (HBsAg)-particles associated with HBe antigen (HBeAg) against soluble polymerized human serum albumin (pHSA), namely albumin receptor, the new enzyme-liked immunosorbent assay (EHSA) using an anti-HBs-coated well of polystyrene microplates and horseradish peroxidase-labelled pHSA was used as an inhibition test using various specific antibodies against human serum components, HB virus (HBV)-associated antigens and liver cell membrane-associated antigens. As the characterization of the bindingsites, all of rabbit antibodies against human serum components, human sera with anti-HBs, human sera with anti-HBe and rabbit antibody against soluble liver specific lipoprotein (anti-LSP) could not bound to the sites, but rabbit anti-HBs, human antibody against non-soluble liver specific membrane antigen (antiLM) and human sera containing both anti-HBs and anti-LM bound to the binding-sites against pHSA.
Rabbit antibody against circulating immune complexes preparated from a patient serum with chronic active hapatitis (CAH) type B (anti-CIC) also bound to the binding-sites. The results of immunofluorescence using FITC-lebelled pHSA and human liver specimens were the same above such as the pHSA could bound to liver cell membranes.
These results indicate that the binding-sites on HBV-particles against pHSA may be associated with LMAg against anti-LM detected in HBsAg-negatve CAH patient sera differed from anti-LSP in both HBsAg-positive and-negative CAH patient sera.
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© The Japan Society of Hepatology
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