Abstract
Antisera, obtained by immunization of rabbits with proteinpolysaccharide complex of human costal cartilage, produced at least two zones of precipitate with antigen on the Ouchterlony assay. The major proteinpolysac-charide fraction, obtained from a DEAE cellulose column chromatography and from a gel filtration, produced a single precipitate line which fused with that of bovine material and therefore was nonspecific between human and bovine material. On the electrophoresis in an agarose gel as well as in a Pevikon powder block, a discrepancy in a mobility occurred between the major glycosaminoglucuronoglycan-containing spot and the antigenic moiety. This antigenic material possessed the chemical composition characteristic to the glycosaminoglucuronoglycan-core protein complex as well as the sialoprotein. After hyaluronidase digestion, this antigenic fragment was characterized rather as a sialoprotein.
