• The Korean Journal of Zoology
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• v.33 no.1
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• pp.103-107
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• 1990

lgM-like immunoglobulin was purified from the immune serum of M albus which immunized with bovine Serum albumin(BSA) as an antigen(Ag) and characterized. The Ag-specific antibody activity of the immune serum was increased after the immunization. The purified lgM-like immunoglobulin had a tetrameric structure which had a molecular weight of 800 kD and the monomer of IgM-like Ig had a mass of 199 kD which was composed of two heavy chains (Mol. wt. 70 kD) and iwo light chains (Mol. wt. 29.5 kD). The IgM-like Ig showed hemaggluti nating activity to mammalian RBC slightly.