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J Gen Virol 63 (1982), 207-212; DOI 10.1099/0022-1317-63-1-207
© 1982 Society for General Microbiology
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Analysis and Purification of Human Lymphoblastoid (Namalwa) Interferon Using a Monoclonal Antibody

G. Allen1, K. H. Fantes1, D. C. Burke2 and J. Morser2

1 Wellcome Research Laboratories, Beckenham, Kent BR3 3BS, U.K.
and2 Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, U.K.

Highly purified interferon-{alpha} (IFN-{alpha}) prepared from a human lymphoblastoid line (Namalwa) was analysed by gel filtration and polyacrylamide gel electrophoresis (PAGE). Gel filtration separated the IFN-{alpha} 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.

Keywords: interferon-{alpha}, Namalwa cells, monoclonal antibody, partial retention

Received 22 March 1982; accepted 28 June 1982.


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