The cloning, expression and crystallisation of a thermostable arginase

Maria C. Bewley, J. Shaun Lott, Edward N. Baker, Mark L. Patchett

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The gene for the thermostable arginase from the thermophilic bacterium 'Bacillus caldovelox' has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in E. coli using an inducible T7 RNA polymerase-based system. A facile purification procedure incorporating a heat-treatment step yielded 0.2 g of recombinant arginase per litre of induced culture. The kinetic properties of the purified recombinant protein are essentially identical to the native enzyme. The recombinant protein has been crystallised and one crystal form is isomorphous to crystals of the native protein.

Original languageEnglish (US)
Pages (from-to)215-218
Number of pages4
JournalFEBS Letters
Volume386
Issue number2-3
DOIs
StatePublished - May 20 1996

Fingerprint

Arginase
Cloning
Crystallization
Organism Cloning
Recombinant Proteins
Crystals
Bacilli
Escherichia coli
Bacillus
Purification
Bacteria
Hot Temperature
Genes
Heat treatment
Kinetics
Enzymes
Proteins
Therapeutics

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Bewley, Maria C. ; Lott, J. Shaun ; Baker, Edward N. ; Patchett, Mark L. / The cloning, expression and crystallisation of a thermostable arginase. In: FEBS Letters. 1996 ; Vol. 386, No. 2-3. pp. 215-218.
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The cloning, expression and crystallisation of a thermostable arginase. / Bewley, Maria C.; Lott, J. Shaun; Baker, Edward N.; Patchett, Mark L.

In: FEBS Letters, Vol. 386, No. 2-3, 20.05.1996, p. 215-218.

Research output: Contribution to journalArticle

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