Analysis and Purification of Human Lymphoblastoid (Namalwa) Interferon Using a Monoclonal Antibody

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Abstract
Highly purified interferon-.alpha. (IFN-.alpha.) prepared from a human lymphoblastoid line (Namalwa) was analyzed by gel filtration and polyacrylamide gel electrophoresis (PAGE). Gel filtration separated the IFN-.alpha. into 2 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 2 major bands by PAGE. The bound fraction (.apprx. 75% of the interferon protein) was purified by means of the monoclonal antibody column, although complete purification of crude interferon was not achieved in 1 passage.