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Abstract Analysis of the glycopeptides of IgA hybridoma proteins by using Tris-borate gels has shown that for mouse α-chain the carbohydrate structure depends on the specificity of the antibody and on the strain of mouse from which the hybridoma was derived. IgA antibodies specific for α1 → 3-linked dextran have sialic acid on all or virtually all of their glycopeptides. IgA antibodies specific for α1 → 6 dextran produced by BALB/c mice have sialic acid only on a small subset of their glycopeptides. However, IgA antibodies specific for α1 → 6 dextran produced by C57BL/6 mice have sialic acid on most of their glycopeptides.
Matsuuchi et al. (1981) studied this question.