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Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 1996

Indoleamine 2,3-dioxygenase: antioxidant enzyme in the human eye.

Сравнительное исследованиеСтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод пока не подготовлен
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Malina H Z, Martin X D

Аннотация

BACKGROUND: Indoleamine 2,3-dioxygenase (IDO) is the first enzyme of the tryptophan degradation pathway. IDO is an antioxidant enzyme because it is a direct scavenger of superoxide radicals. In this study, we measured the activity of IDO in the human eye.

METHODS: IDO was detected in the protein extract of human retina, iris/ciliary body, and lens. The products formed were measured using HPLC with electrochemical detection. Enzyme activity was expressed as the quantity of kynurenine and 3-hydroxykynurenine formed.

RESULTS: IDO activity in the retina extract was 51.5 (+/-10) nmol/g tissue/h, and kynurenine formation was detected. In the iris/ ciliary body, IDO activity was 191.8 (+/49) nmol/g tissue/h, and both kynurenine and 3-hydroxy-kynurenine were formed from tryptophan. In the extract of lens cortex only 3-hydroxykynurenine was formed from tryptophan. IDO activity was 351 (+/-67.3) nmol/g tissue/h.

CONCLUSION: Free tryptophan is degradated in the human eye by IDO, an antioxidative enzyme. IDO may be an antioxidant mechanism in the eye.

Предметные рубрики MeSH

ИП Урсолов Владлен Сергеевич

ИНН 500118482352 · ОГРНИП 314500117700049

Реквизиты и контакты