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.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Tsuchiya M,Osago H,Yamada K,Shimoyama Mdoi
10.1007/978-1-4419-8632-0_30subject
Has Abstractpub_date
1997-01-01 00:00:00pages
245-8eissn
0065-2598issn
2214-8019journal_volume
419pub_type
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