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: The peroxidase-catalyzed oxidation of enkephalins.
    Author: Rosei MA, Blarzino C, Foppoli C, Coccia R, De Marco C.
    Journal: Biochem Biophys Res Commun; 1991 Aug 30; 179(1):147-52. PubMed ID: 1652945.
    Abstract:
    In vitro experiments are reported showing that Leu-enkephalin and Metenkephalin, in the presence of hydrogen peroxide, can be oxidized by horseradish peroxidase. The products formed are strongly fluorescent and characterized by absorption peaks with maxima at 290 nm and 315 nm. The effects of substrate and enzyme concentrations on the oxidation rate of enkephalins are described. Amino acid analysis of the hydrolysates from peroxidase-treated enkephalins provides evidence for the presence of dityrosine. The data suggest that the oxidation leads to the production of enkephalin dimers with a linkage between the N-terminal tyrosine residues. Data are also obtained indicating that enkephalins function as hydrogen donors for mammalian peroxidases.
    [Abstract] [Full Text] [Related] [New Search]