Purification of Rohu Serum Immunoglobulin: A Preliminary Study

Abstract

Attempts were made to purify immunoglobulins from serum of rohu, Labeo rohita, which had been immunised with Edwardsiella tarda. Initially, the proteins in the serum were salted out at 50% saturation with ammonium sulphate and were chromatographed successively by gel filtration and ion exchange columns. The E. tarda agglutination-positive fractions from ion exchange column when concentrated and checked in non-reduced SDS-PAGE, three bands were observed. Since teleost immunoglobulins have been shown to belong to a single class, the two extra bands found in our study might be the degradation products of immunoglobulin or some unpurified contaminants.