Characterisation of arginase from the extreme thermophile 'Bacillus caldovelox'.

@article{Patchett1991CharacterisationOA,
  title={Characterisation of arginase from the extreme thermophile 'Bacillus caldovelox'.},
  author={Mark L. Patchett and Roy M. Daniel and Hugh W. Morgan},
  journal={Biochimica et biophysica acta},
  year={1991},
  volume={1077 3},
  pages={291-8}
}
A thermostable arginase (L-arginine amidinohydrolase, EC 3.5.3.1) was purified from the extreme thermophile 'Bacillus caldovelox' (DSM 411) by a procedure including DEAE-Sepharose chromatography, and gel filtration, anion exchange and hydrophobic-interaction fast-protein liquid chromatography, with substantial retention of the metal ion cofactor. The purified enzyme is a hexamer with a subunit Mr of 31,000 +/- 2000 and contains greater than or equal to 1 Mn atom per subunit. Maximum activation… CONTINUE READING

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