Abstract
Rabbit antisera to calf collagen were investigated using columns of denatured rabbit collagen insolubilized by coupling to diazotized p-aminobenzyl cellulose. Only antibodies with general collagen specificity were bound onto the immunoadsorbent. Species specific antibodies passed through the column and were isolated in the effluent. Column-bound antibodies could be desorbed by elution with collagen peptides. The separated antibody fractions exhibited in haemagglutination—inhibition experiments with calf and rabbit collagen and collagen peptides a characteristic behaviour allowing the differentiation between them. The results support the assumption drawn from serological experiments that most antisera contain mixtures of antibodies with different specificities.
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