Isolation and partial characterization of low sulfated chondroitin 4-sulfate-proteoglycan in bovine blood.
Bovine plasma low sulfated chondroitin sulfate-proteoglycan (34 microgram/ml plasma), accounting for the main component of acidic glycosaminoglycans in blood, has been purified by isoelectric precipitation, dissociation with 4 M guanidine chloride followed by DEAE-chromatography, Sephadex G-200 chromatography and by preparative polyacrylamide gel electrophoresis. The proteoglycan, having a molecular weight of approx. 44,000, is composed of about 77% protein and 23% glycosaminoglycan at a molar ratio of 1 : 1 which could be cleaved by alkaline treatment into each component. Amino acid analysis of the proteoglycan and its glycosylpeptide has shown that the material is derived from a different origin from other tissue proteoglycans, though the amino acid residues surrounding O-glycosidic linkage to serine residue are quite similar to that of cartilage proteoglycan. Characteristic features of plasma low sulfate chondroitin sulfate-proteoglycan are discussed, compared with tissue materials.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D002809:Chondroitin Sulfates / Q000097:blood* / Q000302:isolation & purification; D006025:Glycosaminoglycans / Q000097:blood / Q000302:isolation & purification; D008970:Molecular Weight; D011509:Proteoglycans / Q000097:blood* / Q000302:isolation & purification; D014574:Uronic Acids / Q000032:analysis
D000596:Amino Acids; D006025:Glycosaminoglycans; D011509:Proteoglycans; D014574:Uronic Acids; D002807:Chondroitin; D002809:Chondroitin Sulfates