Affordable Access

Publisher Website

The human interferon-albumin interaction: The influence of albumin conformation

Authors
Journal
Virology
0042-6822
Publisher
Elsevier
Publication Date
Volume
65
Issue
1
Identifiers
DOI: 10.1016/0042-6822(75)90028-8
Disciplines
  • Medicine

Abstract

Abstract When human interferon is chromatographed on bovine serum albumin immobilized via a molecular arm to agarose, there is a selective, transient retention of the interferon. When albumin is defatted prior to immobilization, its interaction with interferon becomes stronger, suggesting that hydrophobic binding is a major force in complex formation. The strength of the interferon-albumin interaction correlates with the extent of deformation of the albumin ligand. Human interferons, induced either by rI n·rC n or Newcastle disease virus (NDV), are retained to the same extent, thus suggesting the existence of common structural features involved in their interactions with immobilized albumin.

There are no comments yet on this publication. Be the first to share your thoughts.