Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1988 Dec 15;256(3):757-62.
doi: 10.1042/bj2560757.

Abilities of peroxidases to catalyse peroxidase-oxidase oxidation of thiols

Affiliations

Abilities of peroxidases to catalyse peroxidase-oxidase oxidation of thiols

B E Svensson. Biochem J. .

Abstract

The abilities of various peroxidases to catalyse the peroxidase-oxidase oxidation of seven aminothiols were studied. Cysteamine and cysteine esters were found to be peroxidase-oxidase substrates for eosinophil peroxidase and myeloperoxidase, whereas other thiols tested were inactive or poorly active with these peroxidases. With lactoperoxidase and horseradish peroxidase, all the tested thiols were inactive or poorly active as peroxidase-oxidase substrates. These studies suggest that a main reason for thiols being poor peroxidase-oxidase substrates is because these thiols are poor peroxidatic substrates.

PubMed Disclaimer

Similar articles

Cited by

References

    1. J Biol Chem. 1981 May 10;256(9):4211-8 - PubMed
    1. Arch Biochem Biophys. 1979 Dec;198(2):580-8 - PubMed
    1. J Reticuloendothel Soc. 1982 Apr;31(4):353-60 - PubMed
    1. Biochemistry. 1982 Aug 31;21(18):4414-9 - PubMed
    1. Biochem Biophys Res Commun. 1983 Nov 15;116(3):873-9 - PubMed