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Biochemical Genetics

, Volume 23, Issue 9–10, pp 771–786 | Cite as

Purification and properties of arylsulfatase B from high- and low-activity mouse strains

  • William L. Daniel
  • Berthie M. Ruoff
  • D. Bruce Thompson
  • Julius B. Gore
Article

Abstract

Arylsulfatase B (arylsulfate sulfohydrolase; EC 3.1.6.1) activities in C57BL/6J, SWR/J, and A/J mouse liver approximate a 5:3:1 ratio. Each enzyme was purified to apparent homogeneity, and the properties of the three purified enzymes were compared. The purified enzyme behaved as a monomer with an apparent molecular weight of 50,000. The purified enzyme catalyzed the hydrolysis ofp-nitrocatechol sulfate (pNCS), 4-methylumbelliferyl sulfate (4MUS), and chondroitin-4-sulfate (C4S) heptasaccharide. Purified SWR/J arylsulfatase B possessed a higher relative electrophoretic mobility atpH 4.0 than the A/J and C57BL/6J isozymes, and the SWR/J enzyme was more thermostable than either the C57BL/6J or the A/J enzyme. No differences were observed among the three enzymes with respect to their Michaelis constants for 4MUS and pNCS, isoelectric points, responses to inhibitors,pH optima, or electrophoretic mobilities atpH 8.3. The relativein vivo rates of synthesis of C57BL/6J, A/J, and SWR/J arylsulfatase B were comparable.

Key words

arylsulfatase chondroitin-4-sulfatase electrophoretic variants house mouse regulation sulfatase 

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References

  1. Agogbua, S. I. O., and Wynn, C. H. (1976). Purification and properties of arylsulfatase B of human liver.Biochem. J. 153415.Google Scholar
  2. Austin, J. H., Balasubramanian, A. S., Pattabiraman, T. N., Saraswathi, S., Basu, D. K., and Bachhawat, B. K. (1963). A controlled study of enzymic activities in three human disorders of glycolipid metabolism.J. Neurochem. 10805.Google Scholar
  3. Balasubramanian, K. A., and Bachawat, B. H. (1976). Partial purification, properties and glycoprotein nature of arysulfatase B from sheep brain.J. Neurochem. 27485.Google Scholar
  4. Berger, F. G., Breen, G. A. M., and Paigen, K. (1979). Genetic determination of the mouse developmental program for mouse liver β-galactosidase: Involvement of sites proximate to and distant from the structural gene.Genetics 921187.Google Scholar
  5. Daniel, W. L. (1976). Genetics of murine liver and kidney arylsulfatase B.Genetics 82477.Google Scholar
  6. Daniel, W. L., and Caplan, M. S. (1980). Comparative biochemistry of murine arylsulfatase B.Biochem. Genet. 18625.Google Scholar
  7. Daniel, W. L., Abedin, K., and Langelan, R. (1980). Murine arylsulfatase B: Evidence favoring control of liver and kidney activity by two regulatory elements.J. Hered. 71161.Google Scholar
  8. Daniel, W. L., Womack, J. E., and Henthorn, P. S. (1981). Murine liver arylsulfatase B processing influenced by region on chromosome 17.Biochem. Genet. 19211.Google Scholar
  9. Daniel, W. L., Harrison, B. W., and Nelson, K. (1982). Genetic regulation of murine hepatic arylsulfatase B activity during development.J. Hered. 7324.Google Scholar
  10. Farooqui, A. A., and Roy, A. B. (1976). The sulphatase of ox liver. XX. The preparation of sulphatases B1 alpha and B1 beta.Biochim. Biophys. Acta 452431.Google Scholar
  11. Farooqui, A. A., and Srivastava, P. N. (1979). Isolation, characterization and the role of rabbit testicular arylsulphatase A in fertilization.Biochem. J. 181331.Google Scholar
  12. Glaser, J. H., and Conrad, H. E. (1979). Chick embryo liver β-glucuronidase: Comparison of activity on natural and artificial substrates.J. Biol. Chem. 2546588.Google Scholar
  13. Goding, J. W. (1976). Conjugation of antibodies with fluorochromes: Modifications to the standard methods.J. Immunol. Methods. 13215.Google Scholar
  14. Gorham, S. D., and Cantz, M. (1978). Arylsulphatase B, an exo-sulphatase for chondroitin 4-sulphate tetrasaccharide.Hoppe-Seyler Z. Physiol. Chem. 3591811.Google Scholar
  15. Hedrick, J. L., and Smith, A. J. (1968). Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis.Arch. Biochem. Biophys. 126155.Google Scholar
  16. Iwamori, M., Moser, H. W., and Kishimoto, Y. (1976). Solubilization and partial purification of steroid sulfatase from rat liver: Characterization of estrone sulfatase.Arch. Biochem. Biophys. 174199.Google Scholar
  17. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of bacteriophage T4.Nature 227680.Google Scholar
  18. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. L. (1951). Protein measurement with the Folin phenol reagent.J. Biol. Chem. 193267.Google Scholar
  19. McGovern, M. M., Vine, D. T., Haskins, M. E., and Desnick, R. J. (1982). Purification and properties of feline and human arylsulfatase B. Evidence for feline homodimeric and human monomeric structures.J. Biol. Chem. 25712605.Google Scholar
  20. Mehl, E., and Jatzkewitz, H. (1968). Cerebroside 3-sulfate as a physiological substrate of arylsulfatase A.Biochim. Biophys. Acta 151619.Google Scholar
  21. Reisfeld, R. A., Lewis, U. J., and Williams, D. E. (1962). Disk electrophoresis of basic proteins and peptides on polyacrylamide gels.Nature 195281.Google Scholar
  22. Rinderknecht, H., Geokas, M. C., Carmack, C., and Haverback, B. J. (1970). The determination of arylsulfates in biological fluids.Clin. Chim. Acta 29481.Google Scholar
  23. Roy, A. B. (1975). L-Ascorbic acid 2-sulfate: A substrate for mammalian arylsulphatases.Biochim. Biophys. Acta 377356.Google Scholar
  24. Shapiro, L. J., Weiss, R., Webster, D., and France, J. T. (1978). X-Linked ichthyosis due to steroid-sulphatase deficiency.Lancet 170.Google Scholar
  25. Smith, K., and Granschow, R. E. (1978). Turnover of murine β-glucuronidase.J. Biol. Chem. 2535437.Google Scholar
  26. Stumpf, D. A., Austin, J. H., Crocker, A. C., and LaFrance, M. (1973). Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome). I. Sulfatase B deficiency in tissues.Am. J. Dis. Child. 126747.Google Scholar
  27. Weber, K., and Osborn, M. (1969). The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.J. Biol. Chem. 2444406.Google Scholar
  28. Womack, J. E., Yan, D. L. S., and Potier, M. (1981). Gene for neuraminidase activity on mouse chromosome 17 near H-2: Pleiotropic effects on multiple hydrolases.Science 21263.Google Scholar

Copyright information

© Plenum Publishing Corporation 1985

Authors and Affiliations

  • William L. Daniel
    • 1
  • Berthie M. Ruoff
    • 1
  • D. Bruce Thompson
    • 1
  • Julius B. Gore
    • 1
  1. 1.Department of Genetics and DevelopmentUniversity of IllinoisUrbana

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