BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Purification and Characterization of Arginase from Schizosaccharomyces pombe

  • Kang, Jung-Hoon (Department of Genetic Engineering, College of Natural Sience & Engineering, Chongju University)
  • Received : 1994.11.14
  • Published : 1995.05.31
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Abstract

Arginase was purified to homogeneity from Schizosaccharomyces pombe. The purified enzyme is a tetramer with a subunit molecular weight of 42,000. Activity is optimal at pH 10.0 and at $60^{\circ}C$ The enzyme migrated during isoelectric focusing showing a pl=5.4. The enzyme exhibited hyperbolic kinetics at pH 10.0 with an apparent $K_m$ for L-arginine of 18 mM. Arginase activity was strongly inhibited by L-glutamate.

Keywords

References

  1. Annu. Rev. Microbiol. v.33 Abdelal, A.T. https://doi.org/10.1146/annurev.mi.33.100179.001035
  2. Acta. Biochim. Pol. v.23 Baranczyk-Kuzma, A.;Poremska, Z.;Mochnacka, I.
  3. Biochem. J. v.175 Beruter, J.;Colombo, J.P.;Bachmann, C. https://doi.org/10.1042/bj1750449
  4. J. Biol. Chem. v.262 Borkovich, K.A.;Weiss, R.L.
  5. Anal. Biochem. v.72 Bardford, M. https://doi.org/10.1016/0003-2697(76)90527-3
  6. Microbiol. Rev. v.50 Davis, R.H.
  7. Schizosaccharomyces Pombe. In Handbook of genetics Gutz, H.;Heslot, H.;Leupold, U.;Loprieno, N.;King, R.C.(ed.)
  8. Eur. J. Biochem. v.25 Harell, D.;Sokolovsky, M. https://doi.org/10.1111/j.1432-1033.1972.tb01673.x
  9. Biochem. J. v.153 Herzfeld, A.;Paper, S.M. https://doi.org/10.1042/bj1530469
  10. Annu. Rev. Genet. v.20 Jackson, M.J.;Beaudet, A.L.;O'Brien, W.E. https://doi.org/10.1146/annurev.ge.20.120186.002243
  11. Arch. Biochem. Biophys. v.95 Jones, M.E.;Andreson, A.D.;Andreson, C.;Hodes, S. https://doi.org/10.1016/0003-9861(61)90182-5
  12. Plant Physiol. v.93 Kang, J.H.;Cho, Y.D. https://doi.org/10.1104/pp.93.3.1230
  13. Nature v.227 Laemmli https://doi.org/10.1038/227680a0
  14. Exp. Cell. Res. v.69 Mitchison, J.M.;Creanor, J. https://doi.org/10.1016/0014-4827(71)90337-5
  15. Biochim. Biophys. Acta. v.118 Mora, J.;Tarrab, R.;Bojalil, L.F. https://doi.org/10.1016/S0926-6593(66)80161-3
  16. Eur. J. Biochem. v.2094 Moreno-Vivian, C.;German, S.;Francisco, C.
  17. Biochim. Biophys. Acta. v.1077 Patchett, M.L.;Daniel, R.M.;Morgan, H.W. https://doi.org/10.1016/0167-4838(91)90543-9
  18. Eur. J. Biochem. v.49 Pennickx, M.;Simon, J.P.;Wiame, J.M. https://doi.org/10.1111/j.1432-1033.1974.tb03848.x
  19. J. Biol. Chem. v.200 Ratner, S.;Pertrack, B.
  20. Methods Enzymol. v.17A Robert, T.S.
  21. Int. J. Pept. Prot. Res. v.22 Rossi, V.;Grandi, C.;Dalzoppo, D.;Fontana, A.
  22. Acta. Biochim. Pol. v.30 Skrzypek-Osiecka, I.;Poremska, Z.
  23. Arch. Biochem. Biophys. v.274 Spolarics, Z.;Bond, J.S. https://doi.org/10.1016/0003-9861(89)90455-4