1887

Abstract

Summary

Highly purified interferon-α (IFN-α) prepared from a human lymphoblastoid line (Namalwa) was analysed by gel filtration and polyacrylamide gel electrophoresis (PAGE). Gel filtration separated the IFN-α into two peaks (A and B). All the components of peak A were retained by a monoclonal antibody (NK2) column, but some of those from peak B were not retained. The IFN that was not bound was active on mouse cells and could be resolved into two major bands by PAGE. The bound fraction (about 75% of the interferon protein) was purified by means of the monoclonal antibody column, although complete purification of crude interferon was not achieved in one passage.

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/content/journal/jgv/10.1099/0022-1317-63-1-207
1982-11-01
2019-11-19
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-63-1-207
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