In atempt to analyze the molecular weight, structure, and subunit components of serum immunoglobulin from snakehead, purification was done by serial procedures ; sodium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 gel filtratio...
In atempt to analyze the molecular weight, structure, and subunit components of serum immunoglobulin from snakehead, purification was done by serial procedures ; sodium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 gel filtration, and Sephadex G-200 gel refiltration. Immunoglobulin titer was detected by the hemagglutination method.
The purified snakehead immnuglobulin was shown a symmetric peak when it was eluted through a Sephadex G-200 containing column and shown a single major band by SDS/3% polyacrylamide-0.5% agarose composite gel electrnphoresis.
The following results were obtained ;
1. The molecular weight of the purified immunoglobulin is about 700,000.
2. The purified immunoglobulin is organized a tetrameric structure of 7 S subunits.
3. The molecular weight of the H-and L-chains are 70,000 and 22,000 resoectively.