Summary
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.
Similar content being viewed by others
Abbreviations
- PAPS:
-
3′phosphoadenosine 5′-phosphosulfate
- chondroitin:
-
totally desulfated chondroitin sulfate
- PPO:
-
2,5-diphenyloxazole
- ΔGlcUA-GalNAc:
-
2-acetamido-2-deoxy-3-0 (β-D-gluco-4-enepyranosyluronic acid)-D-galactose
- ΔGlcUA-GalNAc4S, ΔGlcUA-GalNAc6S and ΔGlcUA-GalNAc4/6S:
-
derivates ΔGlcUA-GalNAc bearing a sulfate at position 4, a sulfate at position 6, and two sulfates at positions 4 and 6, respectively, of the hexosamine moiety
- GlcUA-GalNAc:
-
2 acetamido-2-deoxy-3-O-(β-D-glucopyranosyluronic acid)-D-galactose
- GlcUA-GalNAc4S and GlcUA-GalNAc6S:
-
derivates of GlcUA-GalNAc bearing a sulfate at position 4 and a sulfate at position 6, respectively, of the hexosamine moiety
References
Rodén, L., Baker, J. H., Helting, T., Schwartz, N. B., Stoolmiller, A L., Yamagata, S. and Yamagata, T., 1972. Methods in Enzymology (Ginsburg, V., ed.), Vol. XXVIII, pp. 638–676, Academic Press, New York.
Silbert, J. E. and De Luca, S., 1969. J. Biol. Chem. 244: 876–881.
Richmond, M. E., De Luca, S. and Silbert, J. E., 1973. Biochemistry 12: 3898–3903.
Faltynek, C. R. and Silbert, J. H., 1981. J. Biol. Chem. 256: 7202–7206.
Meezan, E. and Davidson, E. A., 1967. J. Biol. Chem. 242: 1685–1689.
Nakanishi, Y., Shimizu, M., Otsu, K., Kato, S., Tsuji, M. and Suzuki, S., 1981. J. Biol. Chem. 256: 5443–5449.
Suzuki, S. and Strominger, J. L., 1960. J. Biol. Chem. 235: 267–273.
Meyer, K., Linker, A., Davidson, E. A. and Weissmann, B., 1953. J. Biol. Chem. 205: 611–616.
Robbins, P. W., 1962. Methods in Enzymology (Colowick, S. P. and Kaplan, N. O., eds.), Vol. V. pp. 964–977, Academic Press, New York.
Nagasawa, K., Inoue, Y. and Kamata, T., 1977. Carbohydr. Res. 58: 47–55.
Saito, H., Yamagata, T. and Suzuki, S., 1968. J. Biol. Chem. 243: 1536–1542.
Hilborn, J. C. and Anastassiadis, P. A., 1969. Anal. Biochem. 31: 51–55.
Fishman, W. H. and De Lellis, R., 1966. Nature 212: 312.
Baum, H., Dodgson, K. S. and Spencer, B., 1959. Clin. Chim. Acta 4: 453.
Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S., 1968. J. Biol. Chem. 243: 1523–1535.
Rondle, C. J. and Morgan, W. T. J., 1955. Biochem. J. 61: 586–589.
Dische, Z., 1947. J. Biol. Chem. 167: 189–198.
Michelacci, Y. and Dietrich, C. P., 1976. J. Biol. Chem. 251: 1154–1158.
Krystal, G. and Graham, A., 1976. Anal. Biochem. 70: 336–345.
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J., 1951. J. Biol. Chem. 193: 265–275.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Mourão, P.A.S., Salač, M.L.B. The effect of chondroitin sulfate molecular weight and degree of sulfation on the activity of a sulfotransferase from chicken embryo epiphyseal cartilages. Mol Cell Biochem 57, 49–601 (1983). https://doi.org/10.1007/BF00223524
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00223524