| Literature DB >> 16871026 |
Geewook Shin1, Hyungjun Lee, K J Palaksha, Youngrim Kim, Eunyoung Lee, Yongseung Shin, Eunggoo Lee, Kyungdae Park, Taesung Jung.
Abstract
The present study was undertaken to produce monoclonal antibodies (MAbs) against immunoglobulin (Ig) purified from black rockfish (Sebastes schlegeli Higendorf) serum using protein A, mannan binding protein, and goat IgG affinity columns. These three different ligands were found to possess high affinity for black rockfish serum Ig. All of the Igs purified eluted at only 0.46 M NaCl concentration in anion exchange column chromatography and consisted of two bands at 70 kDa and 25 kDa in SDS-PAGE; they also had similar antigenicity for MAbs to Ig heavy chain in immunoblot assays. Therefore, black rockfish Ig is believed to exist as a single isotype within serum. The MAbs produced against Ig heavy chain reacted specifically with spots distributed over the pI range from 4.8 to 5.6 with a molecular weight of 70 kDa on two dimensional gel electrophoresis immunoblot profiles.Entities:
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Year: 2006 PMID: 16871026 PMCID: PMC3242131 DOI: 10.4142/jvs.2006.7.3.293
Source DB: PubMed Journal: J Vet Sci ISSN: 1229-845X Impact factor: 1.672