Partial characterization of serum immunoglobulins of <i>Oreochromis mossambicus</i>

Abstract

Serum immunoglobulins of <i>O. mossambicus </i>were purified using chromatography methods - CM affinity gel blue chromatography followed by two step purification involving a combination of ion-exchange and gel filtration chromatography. Studies revealed that <i>O. mossambicus </i>produces only one class of high molecular weight macroglobulin as determined

by molecular sieving by Sepharose CL 6-B. Immunoelectrophoresis of purified <i>O. mossambicus </i>serum against rabbit anti <i>O. mossambicus </i>serum gave only a single precipitin line. Further analysis of the immunoglobulin by SDS-PAGE showed that<i> </i>the IgM macroglobulin weighs about 900,000 Da, composed of μ-like heavy chain weighing about 90 kDa each and light<i> </i>chains weighing about 30 kDa each.