Isolation and characterization of cartilage proteoglycans immunoreactive with an antibody to skin proteodermatan sulfate core protein.

Low density proteoglycans showing cross-reaction with an antibody to skin proteodermatan sulfate (PDS) core protein were isolated from the bovine articular cartilage, by CsC1 density gradient centrifugation followed by repeated DEAE-cellulose chromatography. The size and amino acid composition of the core proteins of the immunoreactive proteoglycans, eluted at 0.25M and 0.5M NaC1 on DEAE-cellulose column, were quite similar to that of PDS. The glycosaminoglycan components of both proteoglycans were shown to be composed of a hybrid structure of chondroitin sulfate and dermatan sulfate, based on chondroitinase treatments followed by two-dimensional electrophoresis.