Abstract
Summary: The in vivo complexing of albumin with γA-myeloma proteins and Waldenström macroglobulins was investigated. Such complexes were partially purified. Blocking of free sulfhydryl groups in serum proteins was an essential step to prevent dissociation of these complexes during purification. The γA-myeloma protein-albumin complexes and macroglobulin-albumin complexes were not dissociated by 5.0 M guanidine hydrochloride but were dissociated upon reduction by mercaptoethanol. Thus in vivo formed intermolecular disulfide bonds result in the complexes of albumin and γA-globulins and in the complexes of albumin and γM-globulins.