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.
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References
Moss, J., Stanley, S. J. & Watkins, P. A. 1980. Isolation and properties of an NAD-and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255: 5838–5840.
Mishima, K., Terashima, M., Obara, S., Yamada, K., Imai, K. & Shimoyama, M. 1991. Arginine-specific ADP-ribosyltransferase and its acceptor protein p33 in chicken polymorphonuclear cells: co-localization in the cell granules, partial characterization, and In Situ mono(ADP-ribosyl)ation. J. Biochem. 110: 388–394.
Tsuchiya, M., Hara, N., Yamada, K., Osago, H. & Shimoyama, M. 1994. Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells. J. Biol. Chem. 269: 27451–27457.
Soman, G., Tomer, K. B. & Graves, D. J. 1983. Assay of mono ADP-ribosyltransferase activity by using guanylhydrazones. Anal. Biochem. 134: 101–110.
Peterson, J. E., Jacquiline, S.-A. L. & Graves, D. J. 1990. Purification and partial characterization of arginine-specific ADP-ribosyltransferase from skeletal muscle microsomal membranes. J. Biol. Chem. 265: 17602–17609.
Zolkiewska, A. & Moss, J. 1993. Integrin a7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 268: 25273–25276.
Okazaki, I. J., Zolkiewska, A., Nightingale, M. S. & Moss, J. 1994. Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferase. Biochemistry. 33: 12828–12836.
Tsuchiya, M., Osago, H. & Shimoyama, M. 1995. Assay of arginine-specific adenosine-5′-diphosphate-ribosyltransferase by capillary electrophoresis. Anal. Biochem. 224: 486–489.
Tsuchiya, M., Osago, H. & Shimoyama, M. 1995. A newly identified GPI-anchored arginine-specific ADP-ribosyltransferase activity in chicken spleen. Biochem. Biophys. Res. Commun. 214: 760–764.
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© 1997 Springer Science+Business Media New York
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Tsuchiya, M., Osago, H., Yamada, K., Shimoyama, M. (1997). A Newly Identified Glycosylphosphatidylinositol-Anchored Arginine-Specific ADP-Ribosyltransferase in Chicken Spleen. In: Haag, F., Koch-Nolte, F. (eds) ADP-Ribosylation in Animal Tissues. Advances in Experimental Medicine and Biology, vol 419. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8632-0_30
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DOI: https://doi.org/10.1007/978-1-4419-8632-0_30
Publisher Name: Springer, Boston, MA
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