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Protective effects of carnosine, homocarnosine and anserine against peroxyl radical-mediated Cu,Zn-superoxide dismutase modification

Kang JH, Kim KS, Choi SY, et al.. Biochimica et Biophysica Acta, 2002; 1570(2):89-96.

Laboratory studyOther animals

Design
Laboratory study
What was measured
Fragmentation, inactivation, copper release, carbonyl formation and amino acid oxidation of human Cu,Zn-superoxide dismutase exposed to peroxyl radicals from AAPH, with and without carnosine, homocarnosine or anserine.

What the authors reported

AAPH-derived peroxyl radicals fragmented and inactivated Cu,Zn-SOD. Carnosine, homocarnosine and anserine significantly inhibited the fragmentation and inactivation, the release of copper ions, carbonyl formation and oxidation of amino acid residues; they also inhibited fragmentation of a protein lacking copper. The authors attribute the protection to copper chelation and peroxyl radical scavenging.

Limits of this study

In vitro protein chemistry. Abstract only.

Source

PubMed 11985892 · doi:10.1016/s0304-4165(02)00158-7

Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.