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Primate Center TNO, 151 Lange Kleiweg, 2288 GJ Rijswijk, The Netherlands
Two mouse monoclonal antibodies, designated DB-1 and DB-2, were isolated and used for the purification and characterization of recombinant rat interferon gamma (rRIF-
) derived from Chinese hamster ovary (CHO) cells. The two antibodies belong to different classes (DB-1 is an IgG1 and DB-2 an IgA) and display similar epitope specificities as shown in competition binding experiments. Both antibodies, raised against rRIF-, exhibited high affinity for rat and mouse gamma interferon and efficiently neutralized the antiviral activity of both animal interferon species. Affinity chromatography analysis showed that a column with immobilized DB-1 was capable of complete binding of rat and mouse gamma interferon, both natural and recombinant DNA-derived. As visualized by SDS-polyacrylamide gel electrophoresis and Western blot analysis, the purified rRIF- preparation consisted of at least seven molecular forms with Mr values ranging between 14000 and 25000, with a relative abundance of a 18000 Mr protein. Gel permeation chromatography of crude rRIF- gave coincident peaks of rRIF- proteins (all different forms) and interferon activity corresponding to a Mr value of 45000. The results suggest that the molecular heterogeneity was due to differential glycosylation and was not the consequence of a proteolytic degradation process.
Keywords: interferon (rat IFN-), monoclonal antibodies, purification
Received 19 December 1985;
accepted 12 February 1986.
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