Purification and Partial Characterization of α-N-Acetylgalactosaminidase from Porcine Liver

  • Sun-Sang J. Sung
  • Charles C. Sweeley
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 68)


α-N-Acetylgalactosaminidase is an unusual lysosomal glycosidase in that no genetic abnormality involving this enzyme has been discovered. It was discovered many years ago, when Freudenberg and Eichel (1) found that extracts of the hepatopancreas from the snail Helix pomatia inactivated blood group A substance with the release of N-acetylhexosamine and galactose. Cell-free extracts of the flagellate Trichomonas foetus were also observed to contain activity that destroyed blood group A-active glycoprotein (2). Subsequent studies with partially purified preparations from these sources indicated that the loss of serological activity was accompanied by the concomitant liberation of terminal N-acetylgalactosamine (GalNAc) residues (3,4). Terminal GalNAc residues were also released from desialized sheep submaxillary mucin by enzyme fractions from various animal sources (5–7) and Clostridium perfringens (8).


Hydrolase Activity Artificial Substrate Porcine Liver Final Specific Activity Potassium Borate Buffer 


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  1. 1.
    Freudenberg, K., and Eichel, H. (1935) Ann. 518, 97Google Scholar
  2. 2.
    Watkins, W. M. (1959) Biochem. J. 71, 261PubMedGoogle Scholar
  3. 3.
    Tuppy, H., and Staudenbauer, W. L. (1966) Biochemistry 5, 1742PubMedCrossRefGoogle Scholar
  4. 4.
    Harrap, G. J., and Watkins, W. M. (1964) Bioohem. J. 93, 9pGoogle Scholar
  5. 5.
    Schauer, H., and Gottschalk, A. (1968) Bioohim. Biophys. Acta 156, 304CrossRefGoogle Scholar
  6. 6.
    Weissmann, B., and Hinrichsen, D. F. (1969) Biochemistry 8, 2034PubMedCrossRefGoogle Scholar
  7. 7.
    Bhargava, A. S., Buddecke, E., Werries, E., and Gottschalk, A, (1966) Biochim. Biophys. Acta 127, 457PubMedCrossRefGoogle Scholar
  8. 8.
    McGuire, E. J., and Roseman, S. (1967) J. Biol. Chem. 242, 3745PubMedGoogle Scholar
  9. 9.
    Weissmann, B., and Friederici, D. (1966) Biochim. Biophys. Acta 117, 498PubMedCrossRefGoogle Scholar
  10. 10.
    Muramatsu, T. (1968) J. Biochem. (Tokyo) 64, 521Google Scholar
  11. 11.
    Buddecke, E., Schauer, H., Werries, E., and Gottschalk, A. (1969) Biochem. Biophys. Res. Commun. 34, 517PubMedCrossRefGoogle Scholar
  12. 12.
    Weissmann, B., Rowin, G., Marshall, J., and Friederici, D. (1967) Biochemistry 6, 207PubMedCrossRefGoogle Scholar
  13. 13.
    Werries, E., Wollek, E., Gottschalk, A., and Buddecke, E. (1969) Eur. J. Biochem. 10, 445PubMedCrossRefGoogle Scholar
  14. 14.
    Siddiqui, B., and Hakomori, S. (1971) J. Biol. Chem. 246, 5766PubMedGoogle Scholar
  15. 15.
    Sung, S. J., Esselman, W. J., and Sweeley, C. C. (1973) J. Biol. Chem. 248, 6528PubMedGoogle Scholar
  16. 16.
    Gahmberg, C. G., and Hakomori, S. (1975) J. Biol. Chem. 250, 2438PubMedGoogle Scholar
  17. 17.
    Hakomori, S., Stellner, K., and Watanabe, K. (1972) Biochem. Biophys. Res. Commun. 49, 1061PubMedCrossRefGoogle Scholar
  18. 18.
    Smith, E. L., and McKibbin, J. M. (1972) Anal. Biochem. 45, 608PubMedCrossRefGoogle Scholar
  19. 19.
    Slomiany, A., and Horowitz, M. I. (1973) J. Biol. Chem. 248, 6232PubMedGoogle Scholar
  20. 20.
    Slomiany, A., Slomiany, B. L., and Horowitz, M. I. (1974) J. Biol. Chem. 249, 1225PubMedGoogle Scholar
  21. 21.
    Slomiany, B. L., Slomiany, A., and Horowitz, M. I. (1975) Eur. J. Biochem. 56, 353PubMedCrossRefGoogle Scholar
  22. 22.
    Saito, T., and Hakomori, S.-i. (1971) J. Lipid Res. 12, 257PubMedGoogle Scholar
  23. 23.
    Rouser, G., Kritchevsky, G., Yamamoto, A., Simon, G., Galli, C., and Bauman, A. J. (1969) in Methods in Enzymology (Lowenstein, J. M., ed) Vol. XIV, pp. 272, Academic Press, New YorkGoogle Scholar
  24. 24.
    Suzuki, Y., and Suzuki, K. (1972) J. Lipid Res. 13, 687PubMedGoogle Scholar
  25. 25.
    Lloyd, K. O. (1970) Arch. Biochem. Biophys. 137, 460PubMedCrossRefGoogle Scholar
  26. 26.
    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265PubMedGoogle Scholar
  27. 27.
    Vesterberg, O. (1971) in Methods in Enzymology (Jakoby, W. B., ed) Vol. XXII, pp. 389, Academic Press, New YorkGoogle Scholar
  28. 28.
    Gabriel, O. (1971) in Methods in Enzymology (Jakoby, W. B., ed) Vol. XXII, pp. 565, Academic Press, New YorkGoogle Scholar
  29. 29.
    Malik, N., and Berrie, A. (1972) Anal. Biochem. 49, 173PubMedCrossRefGoogle Scholar
  30. 30.
    Bohlen, P., Stein, S., Daireman, W., and Udenfriend, S. (1973) Arch. Biochem. Biophys. 155, 213PubMedCrossRefGoogle Scholar
  31. 31.
    Folch, J., Lees, M., and Sloane-Stanley, G. H. (1957) J. Biol. Chem. 226, 497PubMedGoogle Scholar
  32. 32.
    Israel, M., Bach, G., Miyatake, T., Naiki, M., and Suzuki, K. (1974) J. Neurochem. 23, 803PubMedCrossRefGoogle Scholar
  33. 33.
    Alhadeff, J. A., Miller, A. L., Wenaas, H., Vedvick, T., and O’Brien, J. S. (1975) J. Biol. Chem. 250, 7106PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Sun-Sang J. Sung
    • 1
  • Charles C. Sweeley
    • 1
  1. 1.Department of BiochemistryMichigan State UniversityEast LansingUSA

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