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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

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.

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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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