These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and properties of the Proteus mirabilis catalase.
    Author: Jouve HM, Tessier S, Pelmont J.
    Journal: Can J Biochem Cell Biol; 1983 Jan; 61(1):8-14. PubMed ID: 6342724.
    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.
    [Abstract] [Full Text] [Related] [New Search]