Skip to main content
SpringerLink
Log in

Studies of the purine analog associated modulation of human erythrocyte acid phosphatase activity

  • Original Articles
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

The activity of the human erythrocyte acid phosphatase is modulated by a series of structural analogs of purine. The unsubstituted purine base does not affect the enzyme activity. Addition of a substituent at the number six position usually generates an analog which activates the enzyme while similar substitutions at the two position usually generate an inhibitor. Pyrimidines are generally ineffective as modulators while several modifications of the imidazole ring of the purine analogs do not abolish the modulator activity of the purine analog. The level of response to all active analogs is isozyme specific. Differences in apparent relative affinities among the modulators are noted. The modulators with a positive effect on enzyme activity, are effective in the presence of methanol which is more effective than H20 as a phosphate acceptor. These analogs act by enhancing the rate of transfer of phosphate to H2O, while decreasing the rate of transfer to methanol. The results suggest that the purine analogs may act by altering the rate of hydrolysis of the phosphoenzyme intermediate by H20 or may change the rate-limiting step in the catalytic mechanism.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Fisher RA, Harris H: Further studies of the molecular size of red cell acid phosphatase. Ann Hum Genet Lond 34: 449–453, 1971.

    Google Scholar 

  2. Spencer N, Hopkinson DA, Harris H: Quantitative differences and gene dosage in the human red cell acid phosphatase polymorphism. Nature 201:299–300, 1964.

    Google Scholar 

  3. Eze LC, Tweedie MCK, Bielben MF, Wren PJJ, Evans DAP: Quantitative genetics of human red cell acid phosphatase. Ann Hum Genet Lond 37:333–340, 1974.

    Google Scholar 

  4. Fisher RA, Harris H: Studies on the separate isozymes of red cell acid phosphatase phenotypes A and B. II. Comparison of kinetics and stabilities of the isozymes. Ann Hum Genet Lond 34:439–448, 1971.

    Google Scholar 

  5. Yoshihara CM, Mohrenweiser HW: Characterization of ACP1 ITIC−1, an electrophoretic variant of erythrocyte acid phosphatase restricted to the Ticuna Indians of Central Amazonas. Am J Hum Genet 32:898–907, 1980.

    Google Scholar 

  6. Mohrenweiser HW, Novotny JE: ACP1 GUA-1-A low-activity variant of human erythrocyte acid phosphatase: Association with increased glutathione reductase activity. Am J Hum Genet 34:425–433, 1982.

    Google Scholar 

  7. Luffman JE, Harris H: A comparison of some properties of human red cell acid phosphatase in different phenotypes. Ann Hum Genet 30:387–401, 1967.

    Google Scholar 

  8. Mansfield E, Sensabaugh GF: Red cell acid phosphatase: modulation of activity by purines. In: Brewer GJ (ed), The Red Cell, Vol 4. Alan R Liss, Inc, New York, 1978, pp 233–247.

    Google Scholar 

  9. Mansfield E, Sensabaugh GF: Phenotypic differences in purine modulation of erythrocyte acid phosphatase activity. Lancet 2:201–202, 1977.

    Google Scholar 

  10. Sensabaugh GF, Golden VL: Phenotype dependence in the inhibition of red cell acid phosphatase (ACP) by folates. Am J Hum Genet 30:553–560, 1978.

    Google Scholar 

  11. Naidu JM, Mohrenweiser HW: Erythrocyte acid phosphate: Species specificity in activity modulation by purine analogs. Comp Biochem Phys (in press).

  12. Sensabaugh GF: Genetic and nongenetic variation of human acid phosphatases. In: Markert CL (ed), Isozymes I: Molecular Structure. Academic Press, New York, 1975, pp 367–380.

    Google Scholar 

  13. Lawrence GL, VanEtten RL: The low-molecular-weight acid phosphatase from bovine liver: isolation, amino acid composition, and chemical modification studies. Arch Biochem Biophys 206:122–131, 1981.

    Google Scholar 

  14. Taga EM, VanEtten RL: Human liver acid phosphatase: purification and properties of a low-molecular-weight isoenzyme. Arch Biochem Biophys 214:505–515, 1982.

    Google Scholar 

  15. Rehkop DM, VanEtten, RL: Human liver acid phosphatases. Hoppe-Zeiler's Z Physiol Chem 356:1775–1782, 1975.

    Google Scholar 

  16. Saini MS, VanEtten RL: A homogeneous isozyme of human liver acid phosphatase. Arch Biochem Biophys 191:613–624, 1978.

    Google Scholar 

  17. Chaimovich H, Nome F: Purification and properties of acid phosphatase from bovine brain. Arch Biochem Biophys 139:9–16, 1970.

    Google Scholar 

  18. Swallow DM, Povey S, Harris H: Activity of the ‘red cell’ acid phosphatase locus in other tissues. Ann Hum Genet Lond 37:31–38, 1973.

    Google Scholar 

  19. DiPietro DL, Zengerle FS: Separation and properties of three acid phosphatases from human placenta. J Biol Chem 243:3391–3396, 1967.

    Google Scholar 

  20. Tanizaki MA, Bittencourt HMS, Chaimovich H: Activation of low molecular weight acid phosphatase from bovine brain by purines and glycerol. Biochim Biophys Acta 485:116–123, 1977.

    Google Scholar 

  21. Baldijao CEM, Guija E, Bittencourt HMS, Chaimovich H: Steady state kinetics and the effect of SH inhibitors on acid phosphatase from bovine brain. Biochim Biophys Acta 391:316–325, 1925.

    Google Scholar 

  22. Saini MS, Buchwald SL, VanEtten RL, Knowles JR: Stereochemistry of phospho transfer catalyzed by bovine liver acid phosphatase. Proc Natl Acad Sci USA 256: 10453–10455, 1981.

    Google Scholar 

  23. Fielek S, Mohrenweiser HW: Erythrocyte enzyme deficiencies assessed with a miniature centrifugal analyzer. Clin Chem 25:384–388, 1979.

    Google Scholar 

  24. Neel JV, Mohrenweiser HW, Meisler MM: Rate of spontaneous mutation at human loci encoding protein structure. Proc Natl Acid Sci USA 77:6037–6041, 1980.

    Google Scholar 

  25. Lanzetta PA, Alvarez LJ, Reinach PS, Candia CA: An improved assay for nanomole amounts of inorganic phosphate. Anal Biochem 100:95–97, 1979.

    Google Scholar 

  26. Valentine WN, Tanaka RR, Fredricks RE: Erythrocyte acid phosphatase in health and disease. Am J Clin Pathol 36:328–332, 1961.

    Google Scholar 

  27. Bottini E, Lucarelli P, Bastianon V, Gloria F: Erythrocyte acid phosphatase polymorphism and haemolysis. J Med Genet 9:434–435, 1972.

    Google Scholar 

  28. Bottini E, Scacchi R, Gloria-Bottini F, Mortera J, Palmarino R, Carapella-deLuca E, Lapi AS, Noclari D: Neonatal jaundice and erythrocyte acid phosphatase phenotype. Lancet 1:918, 1976.

    Google Scholar 

  29. Carapella E, Pascone R, Gori MG, Matteucci P, Gloria-Bottini F, Morthera J, Lucarelli P, Scacchi R, Bottini E: The genetic component of quantitative perinatal variables. An analyses of relations between erythrocyte acid phosphatase phenotype and birth weight, gestational age and serum bilirubin level in the first days of life. J Perinat Med 8:42–47, 1980.

    Google Scholar 

  30. Bottini E, Lucarelli P, Agostino R, Palmarino R, Businco L, Antognori G: Favism: association with erythrocyte acid phosphatase phenotype. Science 171:409, 1971.

    Google Scholar 

  31. Bottini E, Carapella E, Orzalesi M, Lucarelli P, Pascone R, Gloria-Bottini F, Coccia M: Is there a role of erythrocyte acid phosphatase polymorphism in intrauterine development. Am J Hum Genet 32:764–767, 1980.

    Google Scholar 

  32. Nichoalds GE, Lawrence JD, Sauberlich HE: Assessment of status of riboflavin nutriture by assay of erythrocyte glutathione reductase activity. Clin Chem 20:624–628, 1974.

    Google Scholar 

  33. Brewster MA, Berry DH, Murphey MN: Automated reaction rate analysis of erythrocyte glucose 6-phosphate dehydrogenase and glutathione reductase activities. Biochem Med 10:229–235, 1974.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Human Genetics, University of Michigan Medical School, 48109-0010, Ann Arbor, MI, USA

    K. Hans Wurzinger, Joseph E. Novotny & Harvey W. Mohrenweiser

Authors
  1. K. Hans Wurzinger
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Joseph E. Novotny
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Harvey W. Mohrenweiser
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wurzinger, K.H., Novotny, J.E. & Mohrenweiser, H.W. Studies of the purine analog associated modulation of human erythrocyte acid phosphatase activity. Mol Cell Biochem 66, 127–136 (1985). https://doi.org/10.1007/BF00220780

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00220780

Keywords

Search

Navigation