ONE-STEP PURIFICATION OF THE MAJOR RAINBOW-TROUT IMMUNOGLOBULIN

Salmonid immunoglobulin purification has been hampered by time-consuming, labour-intensive, conventional chromatographic procedures. In this report we describe the use of immunoaffinity chromatography for the purification of immunoglobulins from trout serum in a single step. An anti-heavy chain monoclonal antibody (1G7) which reacts with more than 85% of total trout immunoglobulins was used to purify the trout immunoglobulin. The purity achieved was higher than 95%, and the immunoglobulins recovered were fully immunogenic. This method served equally well in isolating immunoglobulins from the sera of other salmonids (coho salmon and chinook salmon). The procedure should be useful in the standardization of salmonid immunoglobulin reagents.