Abstract
Publisher Summary DNA recombinants are isolated and identified containing sequences for human leukocyte and fibroblast interferons. One such clone is used to isolate a full-length cDNA recombinant that is reconstructed to express a human leukocyte interferon (IFLrA) in bacteria. With the isolation of 13 monoclonal antibodies to human leukocyte interferon, it is logical to use one or more of them to purify the interferon produced in bacteria. This purification as well as characterization of the bacterial product is described. The monoclonal antibody columns provided major purification of interferon in a single step. Several of the monoclonal antibodies are used to purify IFLrA. These affinity columns provide a convenient method for preparing homogeneous human leukocyte interferon from bacterial fermentations because repeated use of the monoclonal antibody columns is possible. Interferon prepared by modifications of the procedures described is being used in clinical trials in humans. It should be noted that modifications of these procedures are made to obtain a product suitable for parenteral use in humans. The recombinant IFLrA exhibits antiviral activity and antiproliferative activity comparable to crude and purified natural leukocyte interferons.
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