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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000906:Antibodies / Q000276:immunology*; D002358:Cartilage, Articular / Q000032:analysis*; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D003429:Cross Reactions; D003871:Dermatan Sulfate / Q000031:analogs & derivatives* / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D011509:Proteoglycans / Q000276:immunology* / Q000302:isolation & purification*; D012867:Skin / Q000032:analysis*
D000596:Amino Acids; D000906:Antibodies; D011509:Proteoglycans; C028774:proteodermatan sulfate; D003871:Dermatan Sulfate; D002807:Chondroitin