A newly identified GPI-anchored arginine-specific ADP-ribosyltransferase activity in chicken spleen

Arginine-specific ADP-ribosyltransferase activity was detected in chicken spleen membrane fraction and the activity was extracted by phosphatidylinositol-specific phospholipase C but not by 1 M NaCl or 1% Triton X-100. The transferase activity extracted from the spleen membrane was thiol-independent and was not inhibited by 200 mM NaCl. Zymographic analysis of the transferase, under non-reducing conditions, showed two forms of active bands corresponding to a molecular mass of 46 and 42 kDa. Thus, the presence of this novel arginine-specific ADP-ribosyltransferase, anchored to the membrane through glycosylphosphatidylinositol and different from previously cloned chicken transferases, AT1 and AT2, is being given further attention.