Abstract
IgA, IgG and IgM were cleaved by hypochlorous acid treatment. The apparent calculated molecular masses of three polypeptides obtained from IgA were 81.1, 25.8 and 13.9 kDa. The amounts of released IgA fragments were proportional to the amount of HOCl employed. At a HOCl:IgA molar ratio above 320:1, a profound degradation of IgA polypeptide chains occurred, resulting in a yellow-coloured product. The HOC1 treatment of IgG resulted in similar effects, the liberation of three fragments, one of them being of a size slightly larger than that of the light chain (30.4 kDa). The treatment of IgM with HOC1 also produced three fragments: one corresponding to the monomeric IgM molecule, the second to the light chain (26.4 kDa) and the third of a size smaller than the heavy chain. The optimal protein/HOC1 ratios for the degradation of IgG and IgM were 375:1 and 808:1, respectively.
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