Purification and partial characterization of serum immunoglobulins of
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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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The copyright of the articles published in Indian Journal of Fisheries vests with the Indian Council of Agricultural Research, who has the right to enter into any agreement with any organization in India or abroad engaged in reprography, photocopying, storage and dissemination of information contained in these journals. The Council has no objection in using the material, provided the information is being utilized for academic purpose but not for commercial use. Due credit line should be given to the ICAR where information will be utilized.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