The effect of chondroitin sulfate molecular weight and degree of sulfation on the activity of a sulfotransferase from chicken embryo epiphyseal cartilages.
The transfer of [35S] sulfate from [35S]PAPS, by means of PAPS: chondroitin sulfate sulfotransferase, to various chondroitin sulfates, with different degrees of sulfation and molecular weights is reported. Analyses by digestion with chondroitin AC and specific 4- or 6-sulfatases indicate that the sulfation occurs only in position 6 of the non-sulfated N-acetyl galactosamine moiety. The 50-70% desulfated chondroitin 4/6-sulfates are two times better sulfate acceptors than totally desulfated chondroitin, and the affinity of the sulfotransferase increases markedly from the octa-to the deca-saccharide. These results suggest that sulfation increases sharply only after the growing polysaccharide contains about 10 sugar residues, in the early stages of polymerization, and that the sulfation of chondroitin sulfate may be a process in which the addition of some sulfate groups facilitates further sulfation.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002642:Chick Embryo; D002809:Chondroitin Sulfates; D006132:Growth Plate / Q000201:enzymology*; D066298:In Vitro Techniques; D008970:Molecular Weight; D010724:Phosphoadenosine Phosphosulfate; D013379:Substrate Specificity; D013466:Sulfurtransferases / Q000378:metabolism*
D010724:Phosphoadenosine Phosphosulfate; D002809:Chondroitin Sulfates; D013466:Sulfurtransferases