Can I read Interaction between hepatitis B surface proteins and monomeric human serum albumin on EtoBox?

Interaction between hepatitis B surface proteins and monomeric human serum albumin by Bernd Krone; Angela Lenz; Klaus-Hinrich Heermann; Maria Seifer; Lu Xuangyong; Dr. Wolfram H. Gerlich is a Medicine article available to read on EtoBox.

What is Interaction between hepatitis B surface proteins and monomeric human serum albumin about?

HBsAg is known to bind to human serum albumin polymerized by glutaraldehyde, human serum albumin has been found in preparations of HBsAg by several investigators. However, it is not yet known whether natural human serum albumin binds to hepatitis B virus under physiological conditions. We studied the binding between natural or recombinant HBsAg and monomeric human serum albumin by immunological, biochemical and biophysical methods. The binding capacity of 20-nm HBs spheres was variable but ranged up to six molecules HSA/sphere. A reversible binding site for human serum albumin was exclusively localized in the preS2 domain, whereas the S domain was inactive in vitro. Human serum albumin copurified with HBsAg of human origin during gel chromatography or sucrose-gradient centrifugation. This human serum albumin was monomeric in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The preS2-bound part of the human serum albumin could be removed from HBsAg by high-salt, such as CsCl centrifugation, but another part could only be removed by treatment with a disulfide cleaving reagent. Most of this covalently bound human serum albumin was retained at the HBsAg particle after complet

Who reads Interaction between hepatitis B surface proteins and monomeric human serum albumin?

Author

Bernd Krone; Angela Lenz; Klaus-Hinrich Heermann; Maria Seifer; Lu Xuangyong; Dr. Wolfram H. Gerlich

Publisher

Ovid Technologies (Wolters Kluwer Health)

Published

1990

Language

EN

Field

Medicine (Health Sciences)