Characterization of Japanese eel immunoglobulin M and its level in serum |
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Authors: | Uchida D Hirose H Chang P K Aranishi F Hirayabu E Mano N Mitsuya T Prayitno S B Natori M |
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Institution: | Department of Marine Science and Resources, College of Bioresource Sciences, Nihon University, Fujisawa, Japan. |
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Abstract: | Japanese eel immunoglobulin M (IgM) was purified from the sera of Anguilla japonica immunized with Edwardsiella tarda FPU 347 and characterized. Analysis of the purified IgM on sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE) under reducing and non-reducing conditions revealed that the eel IgM was a tetrameric protein with a molecular weight of 790 000; it contained an equimolar heavy chain and light chain with molecular weights of 72 000 and 25 000, respectively. While the N-terminal sequence of the heavy chain, VELTQPGSMVLKPGQSLTI, showed similarity to the variable regions of those of teleost fishes Igs, the N-terminal sequence of the light chain, DIVLTQSPAVQSVQLGDT, was similar to the variable regions of chondrostei and mammalian kappa chains. Lectin-binding assays showed that the binding of concanavalin A (Con A) to the Japanese eel IgM heavy chain was competitively inhibited by
-mannose and could be abolished by α-mannosidase treatment indicating the presence on the heavy chain of oligosaccharides, whose terminal were a bound mannoses. The average IgM concentration in the sera of the healthy eels was 3.4 mg ml−1; it amounted to 10.3% of the total serum protein. |
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Keywords: | Japanese eel Anguilla japonica Immunoglobulin M N-terminal sequence Lectin-binding assay Oligosaccharides with terminal mannoses Single step sandwich ELISA Immunoglobulin M level |
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