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Bu çalışmada, amonyum sülfat çöktürmesi ve Sepharose-4B-L-tirosin-1-aminoantresen jelini içeren hidrofobik etkileşim kromatografisi tekniği kullanılarak insan paraoksonaz (PON1) enzimi saflaştırılmıştır. Saflaştırılan PON1 enziminin saflık kontrolü SDS poliakrilamid jel elektroforezi ile yapılmıştır. Saflaştırma oranı 663 olarak bulunmuştur. Daha sonra saf enzim üzerine metil paration zirai ilacının inhibisyon etkisi incelenmiştir. Söz konusu ilacın IC50 değeri 1,41 mM bulunmuştur.
In this study, the human paraxonase (PON1) enzyme was purified using the hydrophobic interaction chromatography technique containing ammonium sulfate collapse and Sepharose-4B-L-Tyrosin-1-Aminoantresen gel. The purity control of the purified PON1 enzyme is done with SDS polyacrylamide gel electrophoresis. The purification rate was found at 663. The inhibition effect of the methyl paration zirai drug on the pure enzyme was then studied. The IC50 value of the drug was 1.41 mM.
In this study, human paraoxonase (PON1) enzyme was purified by using the hydrophobic interaction chromatography technique including ammonium sulfate precipitation and Sepharose-4B-L-tyrosine-1-aminoantresan gel. The purity control of purified PON1 enzyme was performed by SDS polyacrylamide gel electrophoresis. Purification rate was found to be 663. Then, the inhibition effect of methyl parathion on pure enzyme was investigated. The IC50 value of this compound was 1.41 mM.
Alan : Eğitim Bilimleri; Fen Bilimleri ve Matematik; Mühendislik
Dergi Türü : Ulusal
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