The effect of glycosaminoglycans (GAG) on the intramolecular bindings of collagen.
The subfractions of collagen (alpha, beta and gamma components) precipitated from neutral collagen solution by gelation corresponded to those of collagen precipitated in the same conditions (ion environments) and in the presence of chondroitin-4-sulphate. Collagen fibrils precipitated delayed in the presence of heparin poor in beta chains and rich in alpha chains. The delaying effect of oversulphated GAG on the in vitro fibril formation can be explained by the release or prevention of ion-type intramolecular bonds of collagen. The possible in vivo significance of the above bonds is discussed.
D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002809:Chondroitin Sulfates / Q000494:pharmacology; D003094:Collagen / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006493:Heparin / Q000494:pharmacology; D006820:Hyaluronic Acid / Q000494:pharmacology; D007632:Keratan Sulfate / Q000494:pharmacology
D006025:Glycosaminoglycans; D006820:Hyaluronic Acid; D006493:Heparin; D002809:Chondroitin Sulfates; D003094:Collagen; D007632:Keratan Sulfate