A Newly Identified Glycosylphosphatidylinositol-Anchored Arginine-Specific ADP-Ribosyltransferase in Chicken Spleen

  • Mikako Tsuchiya
  • Harumi Osago
  • Kazuo Yamada
  • Makoto Shimoyama
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 419)


An arginine-specific ADP-ribosyltransferase activity was detected in chicken spleen membrane fraction using a capillary electrophoresis assay and the activity was extracted by phosphatidylinositol-specific phospholipase C but not by 1 M NaCl or 1% Triton X-100. The enzyme protein was purified from chicken spleen membrane fraction to apparent homogeneity with a six-step method containing phosphatidylinositol-specific phospholipase C treatment, ammonium sulfate precipitation and conventional column chromatographies. Apparent molecular mass of the purified enzyme estimated with SDS/PAGE was 44 kDa. N-glycanase treatment of the enzyme reduced the apparent molecular size on SDS/PAGE. The enzyme was recognized by anti-cross reacting determinant antibodies. Partial amino acid sequence of the purified enzyme protein showed high homologies with primary structures of previously reported chicken arginine-specific ADP-ribosyltransferases.


Ammonium Sulfate Precipitation Apparent Molecular Mass Partial Amino Acid Sequence Chicken Spleen Apparent Molecular Size 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Moss, J., Stanley, S. J. & Watkins, P. A. 1980. Isolation and properties of an NAD-and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255: 5838–5840.PubMedGoogle Scholar
  2. 2.
    Mishima, K., Terashima, M., Obara, S., Yamada, K., Imai, K. & Shimoyama, M. 1991. Arginine-specific ADP-ribosyltransferase and its acceptor protein p33 in chicken polymorphonuclear cells: co-localization in the cell granules, partial characterization, and In Situ mono(ADP-ribosyl)ation. J. Biochem. 110: 388–394.PubMedGoogle Scholar
  3. 3.
    Tsuchiya, M., Hara, N., Yamada, K., Osago, H. & Shimoyama, M. 1994. Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells. J. Biol. Chem. 269: 27451–27457.PubMedGoogle Scholar
  4. 4.
    Soman, G., Tomer, K. B. & Graves, D. J. 1983. Assay of mono ADP-ribosyltransferase activity by using guanylhydrazones. Anal. Biochem. 134: 101–110.PubMedCrossRefGoogle Scholar
  5. 5.
    Peterson, J. E., Jacquiline, S.-A. L. & Graves, D. J. 1990. Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes. J. Biol. Chem. 265: 17602–17609.Google Scholar
  6. 6.
    Zolkiewska, A. & Moss, J. 1993. Integrin a7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 268: 25273–25276.PubMedGoogle Scholar
  7. 7.
    Okazaki, I. J., Zolkiewska, A., Nightingale, M. S. & Moss, J. 1994. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferase. Biochemistry. 33: 12828–12836.PubMedCrossRefGoogle Scholar
  8. 8.
    Tsuchiya, M., Osago, H. & Shimoyama, M. 1995. Assay of arginine-specific adenosine-5′-diphosphate-ribosyltransferase by capillary electrophoresis. Anal. Biochem. 224: 486–489.PubMedCrossRefGoogle Scholar
  9. 9.
    Tsuchiya, M., Osago, H. & Shimoyama, M. 1995. A newly identified GPI-anchored arginine-specific ADP-ribosyltransferase activity in chicken spleen. Biochem. Biophys. Res. Commun. 214: 760–764.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Mikako Tsuchiya
    • 1
  • Harumi Osago
    • 1
  • Kazuo Yamada
    • 1
  • Makoto Shimoyama
    • 1
  1. 1.Department of BiochemistryShimane Medical UniversityIzumo 693Japan

Personalised recommendations