Literature DB >> 6342724

Purification and properties of the Proteus mirabilis catalase.

H M Jouve, S Tessier, J Pelmont.   

Abstract

The purification of catalase from Proteus mirabilis has been described. The protein had four subunits of equal apparent molecular weight (MW 62 000). The enzyme was found to be slightly heterogenous after electrofocusing, the main fraction having an isoelectric pH 4.8. No detectable peroxidatic activity was observed in physiological conditions. The absorbance spectrum and the effects of pH and temperature on catalase have also been described.

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Year:  1983        PMID： 6342724     DOI： 10.1139/o83-002

Source DB:  PubMed          Journal:  Can J Biochem Cell Biol        ISSN： 0714-7511


  6 in total

1.  Ligand diffusion in the catalase from Proteus mirabilis: a molecular dynamics study.

Authors:  P Amara; P Andreoletti; H M Jouve; M J Field
Journal:  Protein Sci       Date:  2001-10       Impact factor: 6.725

2.  Cold adapted features of Vibrio salmonicida catalase: characterisation and comparison to the mesophilic counterpart from Proteus mirabilis.

Authors:  Marit Sjo Lorentzen; Elin Moe; Hélène Marie Jouve; Nils Peder Willassen
Journal:  Extremophiles       Date:  2006-04-12       Impact factor: 2.395

3.  Proteus mirabilis urease: genetic organization, regulation, and expression of structural genes.

Authors:  B D Jones; H L Mobley
Journal:  J Bacteriol       Date:  1988-08       Impact factor: 3.490

4.  Occurrence of two different forms of protocatechuate 3,4-dioxygenase in a Moraxella sp.

Authors:  R Sterjiades; J Pelmont
Journal:  Appl Environ Microbiol       Date:  1989-02       Impact factor: 4.792

5.  Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site.

Authors:  A Buzy; V Bracchi; R Sterjiades; J Chroboczek; P Thibault; J Gagnon; H M Jouve; G Hudry-Clergeon
Journal:  J Protein Chem       Date:  1995-02

6.  Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase.

Authors:  O Horner; J-M Mouesca; P L Solari; M Orio; J-L Oddou; P Bonville; H M Jouve
Journal:  J Biol Inorg Chem       Date:  2007-01-20       Impact factor: 3.862
  6 in total

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