Isolation and characterization ofserum immunoglobulins of Cyprinus carpio
2011
SOOD, NEERAJ | RATHORE, GAURAV | SWAMINATHAN, T RAJA | ABIDI, REHANA | MISHRA, B N | LAKRA, W S
unknown. Common carp (Cyprinus carpio) immunoglobulin (Ig) was purified from serum by affinity chromatography using bovine serum albumin as capture ligand. The purified Ig had a molecular weight (MW) of820 kDa as determined by gel filtration chromatography. The MW of heavy and light chain of common carp Ig was 73.7 and 25.3 kDa, respectively, in SDS-PAGE. In no~-reducing SDS..PAGE, 3 bands of different MW were observed, which were presumed to be of different forms of Ig.
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