Two of twenty IgA myeloma proteins studied were found to lack J chain. Both IgA proteins contained dimers and higher polymers (trimers, tetramers, pentamers) in proportions similar to those found in most classical 'J-positive' proteins. Both the 'J-negative' proteins contained bound albumin and alpha-1 antitrypsin (alpha1AT),and reduction with mercaptoethylamine caused a release of albumin and alpha1AT concomitant with depolymerization of the higher polymers of IgA. These proteins formed complexes with secretory component (SC) in vitro, indicating that the presence of J chain is not a requirement for SC binding.