Purification and partial characterization of serum immunoglobulins of


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Authors

  • Neeraj Sood National Bureau of Fish Genetic Resources Canal Ring Road, Lucknow - 226 002, Uttar Pradesh, India
  • T Raja Swaminathan National Bureau of Fish Genetic Resources Canal Ring Road, Lucknow - 226 002, Uttar Pradesh, India
  • Gaurav Rathore National Bureau of Fish Genetic Resources Canal Ring Road, Lucknow - 226 002, Uttar Pradesh, India

Abstract

Channa striatus

immunoglobulin (Ig) was purified from serum by affinity chromatography using bovine serum albumin as

capture ligand. The purified Ig had a molecular weight (MW) of 820 kDa as determined with gel filtration chromatography.

Under reducing SDS-PAGE, the Ig molecule was shown to consist of two subunits, heavy and light chain having a MW of

70.4 and 25.3 kDa, respectively. A high MW band was observed in non-reducing SDS-PAGE, suggesting tetrameric structure.

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How to Cite

Sood, N., Raja Swaminathan, T., & Rathore, G. (2011). Purification and partial characterization of serum immunoglobulins of. Indian Journal of Fisheries, 55(3), 257-260. https://epubs.icar.org.in/index.php/IJF/article/view/6875