Characterization and properties of a lipoprotein-complexing proteoglycan from human aorta

摘要: Abstract The preparation of a proteoglycan (PG) from human aortic intima-media is described. PG was obtained homogenates by differential centrifugation, exclusion chromatography and preparative agarose electrophoresis. Crude or purified preparations the are capable forming specific insoluble complexes with LDL, in serum. This product has been labelled lipoprotein-complexing (LCP-3). On cellulose acetate electrophoresis LCP-3 appears as single band. However, its glycosaminoglycan (GAG) moiety shows composition chromatographic behaviour compatible hybrid mixed chains chondroitin6-SO 4 , dermatan sulfate heparin and/or heparan sulfate. specificity for LDL disappears when it treated testicular hyaluronidase proteolytic enzymes. Ionic strength, pH, Ca ++ Mg modulate amount insolubilized. amino acid protein that basic protein(s), perhaps bound covalently through xylose—serine residues to GAG'S. estimated molecular weight 1 5 × 10 6 daltons. presence interacting at conditions near physiological ones suggestive role this type structure may play associations atherogenic lipoproteins components arterial intima-media.