Isolation and characterization of chondroitin sulfate proteoglycans from porcine thoracic aorta.
A chondroitin sulfate proteoglycan fraction was prepared from the 3 M MgCl2 extract of porcine aortas by DEAE-cellulose chromatography, followed by gel filtration through Sepharose CL-4B. Affinity chromatography of the fraction with antithrombin III-agarose yielded two chondroitin sulfate proteoglycans of a non-binding (proteoglycan IA) and binding (proteoglycan IB) nature. Proteoglycans IA and IB were different from each other in molecular size, in proportion of the protein relative to the polysaccharide portion, and in size of the chondroitin sulfate chain. They were also distinguished immunochemically. These data indicate that the intima-media of the aorta contains at least two distinct species of chondroitin sulfate proteoglycan.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001013:Aorta, Thoracic / Q000032:analysis*; D011508:Chondroitin Sulfate Proteoglycans / Q000276:immunology / Q000302:isolation & purification*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D006025:Glycosaminoglycans / Q000032:analysis; D006909:Hydroxyproline / Q000032:analysis; D008970:Molecular Weight; D011509:Proteoglycans / Q000302:isolation & purification*; D013552:Swine
D000596:Amino Acids; D011508:Chondroitin Sulfate Proteoglycans; D000939:Epitopes; D006025:Glycosaminoglycans; D011509:Proteoglycans; D006909:Hydroxyproline