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 partial characterization of an extracellular aminopeptidase of a collagenolytic bacterium: Empedobacter collagenolyticum].
    Author: Montel MC, Labadie J.
    Journal: Ann Microbiol (Paris); 1982; 133(3):351-63. PubMed ID: 6819795.
    Abstract:
    An aminopeptidase was purified from the culture filtrates of a collagenolytic bacterium Empedobacter collagenolyticum. Purification of this enzyme was accomplished by ammonium sulphate precipitation, gel filtration on Sephadex-G200 and chromatography on DEAE-Sephacel. The purified enzyme seemed homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was about 100,000 daltons as determined by gel filtration on Sephadex-G200 but it was only 33,000 daltons by disc gel electrophoresis in the presence of sodium dodecyl sulphate. This enzyme selectively hydrolysed N-terminal arginine and lysine residues of peptides and arylamides substrates. The enzyme was strongly inhibited by EDTA, ZnCl2 and L-arginine.
    [Abstract] [Full Text] [Related] [New Search]