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Properties of the 3′-phosphoadenosine-5′-phosphosulfate (PAPS) synthesizing systems of brain and liver

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Abstract

Chromatography of brain and liver 100,000g supernatants over HPLC molecular sieve columns revealed striking differences in the molecular weight distribution of ATP-sulfurylase and APS-kinase of the two tissues, pointing to different enzymic species for both enzymes in brain and liver. This was further substantiated by kinetic characterization of the two enzymes of both tissues. APS-kinase of liver is allosterically activated by ATP, while the brain enzyme is not. ATP-sulfurylase of brain is activated at high, but still physiological concentrations of ATP. Brain ATP-sulfurylase is inhibited by phenylalanine.

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References

  1. Levi, A. S., and Wolfe, G. 1969. Purification and properties of the enzyme ATP-sulfurylase and its relation to vitamin A. Biochim. Biophys. Acta 178:262–282.

    Google Scholar 

  2. Burnell, J. N., and Ray, A. B. 1978. Purification and properties of the ATP-sulfurylase of rat liver. Biochim. Biophys. Acta 572:239–248.

    Google Scholar 

  3. Shoyab, M., Su, L. Y., and Marx, W. 1972. Purification and properties of ATP-sulfurylase from Furth mouse mastocytoma. Biochim. Biophys. Acta 258:113–124.

    Google Scholar 

  4. Suguhara, K., and Schwartz, N. B. 1982. Defect in 3′-phosphoadenosine-5′-phosphosulfate synthesis in brachymorphic mice. I. Characterization of the defect. Arch. Biochem. Biophys. 214:589–601.

    Google Scholar 

  5. Suguhara, K., and Schwartz, N. B. 1982. Defect in 3′-phosphoadenosine 5′-phosphosulfate synthesis in brachymorphic mice. II. Tissue distribution of the defect. Arch. Biochem. Biophys. 214:602–609.

    Google Scholar 

  6. Hommes, F. A. 1985. Myelin turnover at later stages of brain development in experimental hyperphenylalaninemia. Pages 67–85, in Bickel, H., and Wachtel, U. (eds.), Inherited diseases of amino acid metabolism. Recent progress in the understanding, recognition and management. Thieme, Stuttgart.

    Google Scholar 

  7. Hommes, F. A., and Moss, L. 1986. The assay of ATP-sulfurylase. Anal. Biochem. 154:100–104.

    Google Scholar 

  8. Robbins, P. W. 1962. Sulfate activating enzymes. Meth. Enzymol. 5:964–977.

    Google Scholar 

  9. Gregory, J. D. 1962. Sulfate transferring enzymes. Meth. Enzymol. 5:977–983.

    Google Scholar 

  10. Lowry, O. H., Rosebrough, N., Farr, L. A., and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.

    Google Scholar 

  11. Shoyab, M., and Marx, W. 1972. Enzyme substrate complexes of ATP-sulfurylase from mouse mastocytoma. Biochim. Biophys. Acta 258:125–132.

    Google Scholar 

  12. Lowry, O. H., Passoneau, J. V., Hasselberger, F. X., and Schulz, D. W. 1964. Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain. J. Biol. Chem. 239:18–30.

    Google Scholar 

  13. Gaull, G. E., Tallan, H. H., Lajtha, A., and Rassin, D. K. 1975. Pathogenesis of brain dysfunction in inborn errors of amino acid metabolism. Pages 47–143 in Gaull, G. E. (ed.), Biology of brain development. Plenum, New York, Vol. 1.

    Google Scholar 

  14. Chase, H. P., and O'Brien, D. 1970. Effect of excess phenylalanine and of other amino acids on brain development in the infant rat. Pediatr. Res. 4:96–102.

    Google Scholar 

  15. London, Y., Demel, R. A., Geurts van Kessel, W. S. M., Vossenberg, F. G. A., and Van Deenen, L. L. M. 1973. The protection of A1 myelin basic protein against the action of proteolytic enzymes after interaction of the protein with lipids at the air water interface. Biochim. Biophys. Acta 311:520–530.

    Google Scholar 

  16. London, Y., and Vossenberg, F. G. A. 1973. Specific interactions of central nervous system myelin basic protein with lipids. Specific regions of the protein action of trypsin. Biochim. Biophys. Acta. 307:478–490.

    Google Scholar 

  17. Berger, R., Springer, J., and Hommes, F. A. 1980. Brain protein and myelin metabolism in young hyperphenylalaninemic rats. Mol. Cell Biol. 26:31–36.

    Google Scholar 

  18. Hommes, F. A., Eller, A. G., and Taylor, E. H. 1982. The effect of phenylalanine on myelin metabolism in adolescent rats. Pages 193–199, in Cockburn, F. and Gitzelmann, R. (eds.). Inborn errors of metabolism in humans, MTP Press, Lancaster.

    Google Scholar 

  19. Hommes, F. A., Eller, A. G., and Taylor, E. H. 1982. Turnover of the fast component of myelin and myelin proteins in experimental hyperphenylalaninemia. Relevance to termination of dietary treatment. J. Inher. Metab. Dis. 5:21–27.

    Google Scholar 

  20. Taylor, E. H., and Hommes, F. A. 1983. Effect of experimental hyperphenylalaninemia on myelin metabolism at later stages of brain maturation. Int. J. Neurosci. 20:257–228.

    Google Scholar 

  21. Matsuo, K., Moss, L., and Hommes, F. A. 1986. The development of ATP-sulfurylase and APS-kinase in rat cerebrum and liver. Submitted for publication.

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Matsuo, K., Moss, L. & Hommes, F.A. Properties of the 3′-phosphoadenosine-5′-phosphosulfate (PAPS) synthesizing systems of brain and liver. Neurochem Res 12, 345–349 (1987). https://doi.org/10.1007/BF00993243

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