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
Interaction of hepatitis B surface antigen with polymerized human serum albumin
โ Scribed by Sean P. O'Neill
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 492 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0146-6615
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โฆ Synopsis
Abstract
HBsAg binds to a solidโphase 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 human serum, suggesting significant attachment of serum components at the locations on HBsAg particles where polymerized HSA binds. The temperature dependence of the interaction goes through a maximum above room temperature, in contrast to the increasing reaction with temperature of the HBsAgโantiโHBs antibody system. The interaction between HBsAg and polymerized HSA is discussed in relation to previous findings of HSA polymers and antiโpolyโmerized albumin antibodies in hepatic patients. A mechanism for production of an autoimmune, antialbumin antibody condition, in association with hepatitis B virus infection is proposed.
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