A newly identified glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase in chicken spleen.
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.
Tsuchiya
M
M
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
Osago
H
H
Yamada
K
K
Shimoyama
M
M
D036002:ADP Ribose Transferases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D002645:Chickens; D006026:Glycoside Hydrolases / Q000378:metabolism; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D013154:Spleen / Q000201:enzymology*
D017261:Glycosylphosphatidylinositols; D009243:NAD; D001120:Arginine; D036002:ADP Ribose Transferases; D006026:Glycoside Hydrolases; C020668:glycanase