Purification and some properties of urate oxidase from nitrogen-fixing nodules of cowpea

Biochim Biophys Acta. 1981 May 14;659(1):132-40. doi: 10.1016/0005-2744(81)90277-1.

Abstract

Urate oxidase (urate: oxygen oxidoreductase, EC 1.7.3.3) was purified 166-fold from nitrogen-fixing root nodules of cowpea Vigna unguiculata [L.] Walp. The purified enzyme showed a specific activity of 5.7 mumol urate oxidised/min per mg protein, a molecular mass of 100 kdaltons, pH optimum between 9 and 10, isoelectric point at PH 6.8, Km(urate) = 18 muM and Km(oxygen) = 29 muM. A number of metal complexing and chelating reagents were inhibitory, as were divalent cations, including Cu2+. Iron stimulated the enzyme. Low concentrations of ammonia, glutamine and xanthine were also inhibitory. The regulation of urate oxidase in relation to the assimilation of fixed nitrogen in legume nodules is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonia / pharmacology
  • Cations, Divalent / pharmacology
  • Fabaceae
  • Glutamine / pharmacology
  • Isoelectric Point
  • Metals / pharmacology
  • Molecular Weight
  • Nitrogen Fixation*
  • Plants / enzymology*
  • Plants, Medicinal
  • Urate Oxidase / isolation & purification*
  • Xanthines / pharmacology

Substances

  • Cations, Divalent
  • Metals
  • Xanthines
  • Glutamine
  • Ammonia
  • Urate Oxidase