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)

Abstract

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.

Keywords

Phenyl Electrophoresis Arginine Turkey Disulfide 

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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

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