CHARACTERIZATION OF TWO STRUCTURALLY RELATED PROTEOCHONDROITINSULFATES FROM A HUMAN B LYMPHOBLASTOID CELL LINE

Abstract

Twodifferent proteochondroitinsulfates were purified from culture supernatant andcellular lysate of the human B-lymphoblastoid cell line LICR-LON-HMy2. The proteoglycansconsist of a comparatively small protein core (supernatantproteoglycan: 21,5 kDa, cell surface proteoglycan: 30 kDa) to whichthree to four chondroitinsulfate chains (CS-4-sulfate and CS-6-sulfate), each of 26 to 30 kDa are attached. The molecular massof the mature proteoglycan wasestimated as approximately 130-150 kDa. Both proteochondroitinsulfates could be distinguished by a different structure of the protein core which became apparentafter amino acid analysis and comparative peptide mapping. In contrast to the cell surface proteoglycan, the protein core of the supernatant proteoglycan contained additionally N-linked oligosaccharides.