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Glutatyon redüktaz (GR), NADPH'ye bağlı oksidoredüktaz ailesinde bulunur. GR hücrede protein ve DNA biyosentezi, reaktif oksijen türlerinin ve serbest radikallerin detoksifikasyonu gibi çeşitli önemli fonksiyonlara sahiptir. Bu çalışmanın amacı, GR enzimi üzerine antiepileptik ilaçların (fenintoin, gabapentin ve pirimidon) in vitro etkilerini belirlemektir. Bu çalışmada, GR enzimi insan eritrositlerinden 20.08 EU/mg protein spesifik aktivite ve 2135.97 kat saflaştırıldı. Anti-epileptik ilaçların GR enzimi üzerindeki inhibisyon etkisini belirlemek için Lineweaver-Burk grafikleri çizildi Ki sabiti ve inhibisyon tipleri bu çizilen grafiklerden hesaplandı. Ki değerleri 0.15± 0.03-5.74±1.14 mM aralığında bulundu. Fenintoin en etkili inhibitör özelliğini yarışmalı inhibisyon tipi ile göstermiştir.
Glutation reductaze (GR) is found in the NADPH-related oxideductaze family. GR cells have a variety of important functions, such as protein and DNA biosynthesis, the detoxification of reactive oxygen and free radicals. The aim of this study is to determine the in vitro effects of antiepileptic drugs (fenintoin, gabapentin and pirimidon) on the GR enzyme. In this study, the enzyme GR was purified 20.08 times the specific activity of the EU/mg protein and 2135.97 times the human erythrosites. Lineweaver-Burk graphs were drawn to determine the inhibitory effect of anti-epileptic drugs on the GR enzyme; the stability and types of inhibition were calculated from these drawn graphs. Ki values were found in the range of 0.15± 0.03-5.74±1.14 mM. The most effective inhibitor characteristics of fenintoin have been shown by the competitive type of inhibition.
Glutathione reductase (GR) is found in the NADPH-dependent oxidoreductase family. GR has various important functions in the cell, such as protein and DNA biosynthesis, the detoxification of reactive oxygen species and free radicals. The purpose of this research was to perform the in vitro inhibition effects of anti-epileptic drugs (phenytoin, gabapentin, and primidone) on GR enzyme. In the current study, the GR enzyme was purified from human erythrocytes with a specific activity of 20.08 EU/mg protein and 2135.97-purification fold. To determine the inhibition effects of anti-epileptic drugs on GR enzyme, Lineweaver-Burk graphs were drawn for each inhibitor. Ki values and inhibition types were determined from these plotted graphs. The Ki values of drugs were found in ranging from 0.15± 0.03-5.74±1.14 mM. Phenytoin was shown the most effective inhibitor feature with a competitive inhibition type.
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