A new method was established for a high yield of purified IgD by using ion exchange chromatography under the conditions where the IgD protein was not absorbed.
Despite the buffer containing 0.01M ε-amino caproic acid was used to protect against proteolysis, spontaneous degradation of IgD occured during purification step at 4°C. The molecular weight of this degradation fragment was about 123, 000 daltons determined by SDS-PAGE. It was, therefore, probable that the fragments were F (ab)
2δ or the dimer of Fcδ and Fabδ.
For the study of the reactivity aginst Fabδ portion, specific rabbit anti-IgD antibody was prepared and compared with those supplied commercially. The results indicated that the latter did not show any reaction against Fabδ, suggesting that it may lack the antibody against Fdδ.
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