
Serum immunoglobulins of O. mossambicus 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 O. mossambicus produces only one class of high molecular weight macroglobulin as determined by molecular sieving by Sepharose CL 6-B. Immunoelectrophoresis of purified O. mossambicus serum against rabbit anti O. mossambicus serum gave only a single precipitin line. Further analysis of the immunoglobulin by SDS-PAGE showed that the IgM macroglobulin weighs about 900,000 Da, composed of mu-like heavy chain weighing about 90 kDa each and light chains weighing about 30 kDa each.
Immunoglobulins, Serum Albumin, Bovine, Hemagglutination Tests, Blood Protein Electrophoresis, Chromatography, Ion Exchange, Molecular Weight, Precipitins, Immunoglobulin M, Chromatography, Gel, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Immunization, Rabbits, Immunoelectrophoresis, Tilapia
Immunoglobulins, Serum Albumin, Bovine, Hemagglutination Tests, Blood Protein Electrophoresis, Chromatography, Ion Exchange, Molecular Weight, Precipitins, Immunoglobulin M, Chromatography, Gel, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Immunization, Rabbits, Immunoelectrophoresis, Tilapia
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