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pubmed-article:10520725pubmed:dateCreated1999-11-10lld:pubmed
pubmed-article:10520725pubmed:abstractTextIt is well known that aminoguanidine (AG) can diminish advanced glycosylation of proteins, which might be beneficial in preventing chronic diabetic complications. Recent reports suggested an inter-relationship between glycosylation of protein and free radical damage. In the present study, we examined the free radical scavenging properties of AG. Electron paramagnetic resonance using the spin-trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) was performed to determine the superoxide and hydroxyl radical scavenging abilities of AG. These experiments revealed that AG was an effective hydroxyl radical scavenger even though it expressed a direct inhibitory effect on the xanthine oxidase activity at high concentrations (AG > or = 5 mM). In the second part of the study, allophycocyanin was used as an indicator of free radical mediated protein damage. In the assay, 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH) was used as a peroxyl radical generator, and the loss of allophycocyanin fluorescence was monitored. The antioxidant effect of AG was expressed in oxygen-radical absorbing capacity (ORAC), where one ORAC unit equals the net protection produced by 1 microM Trolox (a water soluble analogue of vitamin E) as a control standard. AG exhibited a significant dose-dependent effect against free radical damage. These radical scavenging properties of AG may contribute to protective effects during glycation and explain the prevention of diabetic complications.lld:pubmed
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pubmed-article:10520725pubmed:pagination535-40lld:pubmed
pubmed-article:10520725pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:10520725pubmed:year1999lld:pubmed
pubmed-article:10520725pubmed:articleTitleAntioxidant properties of aminoguanidine.lld:pubmed
pubmed-article:10520725pubmed:affiliationLPPCE, Facultés de Médecine et Pharmacie, Dijon, France.lld:pubmed
pubmed-article:10520725pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10520725pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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