Biochemical Genetics

, Volume 25, Issue 11–12, pp 901–918 | Cite as

Immunochemical characterization of human red cell acid phosphatase isozymes

  • J. Dissing


An immunological study was performed on human red cell acid phosphatase (ACP1) isozymes encoded by different alleles, each of which is expressed as an electrophoretically fast (f) isozyme and a slow (s) isozyme. These isozymes reacted as two immunochemically different groups. Allele-specific reactions were not detected between either the f isozymes or the s isozymes. Quantitation of ACP1 isozymes in red cells by crossed immunoelectrophoresis revealed a phenotype-dependent variation in the concentration of isozyme protein. A simple gene dosage effect was indicated and the ordering of the ACP1 alleles (ACP1*A < ACP1*B < ACP1*C < ACP1*E) was identical to that found for enzyme activity levels. Also, an allele effect on the proportion between s and f isozymes (s/f) was observed; the ordering here was ACP1* B < ACP1*A < ACP1*, which is the same as that reported for the susceptibility to modulation with purines. These variations in isozyme protein levels appear to account for the phenotypic differences in the intensity of the isozyme bands, when activity-stained after electrophoresis, and in the red cell enzyme activity levels. Investigation of two carriers of a Null allele showed no evidence of an aberrant protein product, and half-normal concentrations of enzyme protein were observed in the red cells of these individuals.

Key words

erythrocyte acid phosphatase (ACP1) isozymes immunochemical properties quantitation 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Axelsen, N. H., and Bock, E. (1983). Electroimmunoassay (rocket immunoelectrophoresis). Scand. J. Immunol 17 (Suppl. 10):103.Google Scholar
  2. Dissing, J. (1981). Human red cell acid phosphatase: Differences in concentration of isozymeprotein as cause of phenotypic differences in enzyme activity. In Gathof, A. G. (ed.), Proc. 9th Int. Congr. Soc. Forensic Haemogenet., Bern,Sept. 29-Oct. 3, 1981 Schmitt and Meyer, Würzburg, pp. 279–283.Google Scholar
  3. Dissing, J. (1986). Red cell acid phosphatase: Only two different enzymes—the “slow” and the “fast” enzyme—determine different biochemical properties of the six common phenotypes. In Brinkmann, B., and Henningsen, K. (eds.), Advances in Forensic Haemogenetics Springer-Verlag, Berlin, Heidelberg, New York, Tokyo, Vol. 1, pp. 127–131.Google Scholar
  4. Dissing, J., and Svensmark, O. (1976). Human red cell acid phosphatase: Quantitative evidence of a silent gene P, and a Danish population study. Hum. Hered. 2643.Google Scholar
  5. Dissing, J., and Bär, W. (1985). Studies on the electrophoretic separation of the four common human phosphoglucomutase (PGM1) allozymes. Electrophoresis 6583.Google Scholar
  6. Dissing, J., and Sensabaugh, G. F. (1987). Human red cell acid phosphatase: Evidence for differences in the primary structure of the two isozymes expressed by the ACP1*B allele. Biochem. Genet. 25919.Google Scholar
  7. Dissing, J., Dahl, O., and Svensmark, O. (1979). Phosphonic and arsonic acids as inhibitors of human red cell acid phosphatase and their use in affinity chromatography. Biochim. Biophys. Acta 569159.Google Scholar
  8. Eze, L. C., Tweedie, M. C. K., Bullen, M. F., Wren, P. J. J., and Evans, D. A. P. (1974). Quantitative genetics of human red cell acid phosphatase. Ann. Hum. Genet. 37333.Google Scholar
  9. Fenton, M. R., and Richardson, K. E. (1971). Human erythrocyte acid phosphatase: Resolution and characterization of the isozymes from three homozygous phenotypes. Arch. Biochem. Biophys. 14213.Google Scholar
  10. Fisher, R. A., and Harris, H. (1969). Studies on the purification and properties of the genetic variants of red cell acid phosphatase in man. Ann. N.Y. Acad. Sci. 166380.Google Scholar
  11. Fisher, R.A., and Harris, H. (1971a). Studies on the separate isozymes of human red cell acid phosphatase phenotypes A and B. Ann. Hum. Genet. 34439.Google Scholar
  12. Fisher, R. A., and Harris, H. (1971b). Further studies on the molecular size of red cell acid phosphatase. Ann. Hum. Genet. 34449.Google Scholar
  13. Harboe, N., and Ingild, A. (1973). Immunization, isolation of immunoglobulins, estimation of antibody titre. In Axelsen, N. H., Krøll, J., and Weeke, B. (eds.) Quantitative Immunoelectrophoresis Universitetsforlaget, Oslo, pp. 161–164.Google Scholar
  14. Harboe, N. M. G., and Ingild, A. (1983). Immunization, isolation of immunoglobulins and antibody titre determination. Scand. J. Immunol. 17 (Suppl. 10):345.Google Scholar
  15. Harris, H. (1980). The Principles of Human Biochemical Genetics Elsevier/North-Holland, Amsterdam, New York, Oxford, pp. 190–197.Google Scholar
  16. Hopkinson, D. A., Spencer, N., and Harris, H. (1963). Red cell acid phosphatase variants: A new human polymorphism. Nature 199969.Google Scholar
  17. Hopkinson, D. A., Spencer, N. and Harris, H. (1964). Genetical studies on human red cell acid phosphatase. Am. J. Hum. Genet 16141.Google Scholar
  18. Mansfield, E., and Sensabaugh, G. F. (1978). Red cell acid phosphatase: Modulation of activity by purines. In Brewer, G. J. (ed.), The Red Cell Alan R. Liss, New York, Vol. 4, pp. 233–247.Google Scholar
  19. Ouchterlony, O. (1953). Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol. Microbiol. Scand. 32231.Google Scholar
  20. Peterson, G. L. (1977). A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83346.Google Scholar
  21. Sensabaugh, G. F., and Golden, V. L. (1978). Phenotype dependence in the inhibition of red cell acid phosphatase (ACP) by folates. Am. J. Hum. Genet. 30553.Google Scholar
  22. Spencer, N., Hopkinson, D. A., and Harris, H. (1964). Quantitative differences and gene dosage in the human red cell acid phosphatase polymorphism. Nature 201299.Google Scholar
  23. Sørensen, S. A. (1975). Report and characterization of a new variant, EB, of human red cell acid phosphatase. Am. J. Hum. Genet. 27100.Google Scholar
  24. Svendsen, P. J., Weeke, B., and Johansson, B.-G. (1983). Chemicals, solutions, equipment and general procedures. Scand. J. Immunol. 17 (Suppl. 10):3.Google Scholar
  25. White, I. N. H., and Butterworth, P. J. (1971a). Isoenzymes of human erythrocyte acid phosphatase. Biochim. Biophys. Acta 229193.Google Scholar
  26. White, I. N. H., and Butterworth, P. J. (1971b). A comparison of the stabilities of the isoenzymes of human erythrocyte acid phosphatase (type B). Biochim. Biophys. Acta 229202.Google Scholar

Copyright information

© Plenum Publishing Corporation 1987

Authors and Affiliations

  • J. Dissing
    • 1
  1. 1.Institute of Forensic GeneticsUniversity of CopenhagenCopenhagenDenmark

Personalised recommendations