## Abstract HBsAg binds to a solidβphase adsorbent consisting of polymerized human serum albumin (HSA) on glass particles. Both AD and AY antigenic subtypes of hepatitis B surface antigen (HBsAg) display this interaction. In either case, the binding to polymerized HSA is reduced in the presence of
Interaction of hepatitis B surface antigen with serum albumin of various species on polystylene latex particles
β Scribed by Y. Ise; M. Fukuda; T. Suzuki
- Publisher
- Springer-Verlag
- Year
- 1987
- Tongue
- English
- Weight
- 658 KB
- Volume
- 176
- Category
- Article
- ISSN
- 0300-8584
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β¦ Synopsis
Polystylene latex particles coated with serum albumin of various species, including non-primate serum albumin, were agglutinated by sera containing hepatitis B surface (HBs) antigen and hepatitis Be (HBe) antigen and by purified HBs antigen. Monomer and polymer albumin separated from human serum albumin preparations on latex particles were found to react with HBs antigen. Monomer from non-primate serum albumin preparations bound to latex particles was also found to have the ability to react with HBs antigen, but polymer of non-primate serum albumin did not. The mechanism of reaction between HBs antigen and the latex-bound serum albumin of various species is discussed.
π SIMILAR VOLUMES
Receptors for polymerised human albumin are present on the pre-S sequence of the envelope protein of HBV and on the hepatocyte membrane and are thought to be involved in uptake of the virus by hepatocytes. Using a solid phase radioimmunoassay we demonstrate binding of HBsAg to polymerised human seru