Protein HC‐IgA Complexes Carry Antibody Activities

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Abstract
Polyclonal protein HC-IgA complexes (HC-IgA) were isolated from two different serum pools. Their hydrodynamic volumes were found to be slightly greater than that of monomeric IgA but less than that of dimeric IgA. Sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis of reduced and carboxymethylated complexes followed by immunoblotting showed that the complexes contained normal light and heavy Ig chains, and one polypeptide chain with Mr = 90,000, which carried both IgA .alpha. chain and protein HC epitopes. Enzyme-linked immunosorbent assays (ELISA) demonstrated that the isolated HC-IgA carried about 0.1 and 4% respectively, of the antibody activities against one carbohydrate antigen (Yersinia enterocolitica serotype 0:3 lipopolysaccharide) and one protein antigen (rabbit IgG, i.e. antigen for rheumatoid factors) of the IgA populations of the two serum pools. HC-IgA with rheumatoid factor activity could also be demonstrated in the unfractionated serum pool. The binding of HC-IgA in the ELISA was not mediated through its protein HC part. The present observations show that HC-IgA carries antibody activities and constitutes a unique class of IgA complexes, since it does not dissociate under denaturing conditions after reduction. It may represent a further biological potential of the humoral immune system.