CHARACTERIZATION OF E ANTIGEN ASSOCIATED WITH HEPATITIS-B

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 35  (3) , 380-389
Abstract
Hepatitis B e antigen (HBe) from the serum of a chronic carrier of HBsAg [hepatitis B surface antigen] was partially purified and characterized. It behaves as an acidic protein, pI [isoelectric point] 4.5-5.0, which is thermolabile and sulfhydryl-sensitive. In serum it usually has a flotation density 1.3 g/cm3, but is sometimes found at density 1.15 g/cm3 because of its association with lipid. HBe from serum is polydisperse on gel filtration although most antigen is recovered with a nominal MW of 3 .times. 105 daltons. In the presence of chaotropic ions, the bulk of serum HBe is found as a species of 3 .times. 104 daltons previously detected in small amounts under non-dissociating conditions. This suggests that the larger material is formed by non-covalent association of the 3 .times. 104 dalton species with itself or other serum components. This would include Ig[immunoglobulin]G, although there is no evidence that HBe itself bears Ig determinants. Analysis of HBe precipitins by polyacrylamide gel electrophoresis under reducing and dissociating conditions suggests that its component polypeptide chains are about 1.7 .times. 104 daltons.