Lipoksigenaz Enziminin Sığır Karaciğerinden Kısmi Saflaştırılması, Karakterizasyonu, Salisilik Asitin ve Bazı Flavonların Enzim Üzerine Etkileri

ÖZTÜRK KESEBİR A., KILIÇ D., KÜFREVİOĞLU Ö. İ.

Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi, cilt.9, sa.3, ss.1452-1459, 2019 (Hakemli Dergi)

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 9 Sayı: 3
  • Basım Tarihi: 2019
  • Dergi Adı: Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi
  • Derginin Tarandığı İndeksler: TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.1452-1459
  • Atatürk Üniversitesi Adresli: Evet

Özet

Lipoxygenase (EC 1.13.11.34; LOX) is a non-hem iron-bearing dioxygenase which converts oxygen into fatty acids containing two or more unsaturated bonds and converts them into fatty acid hydroperoxides. Lipoxygenase activity is described in developed plants, in mammals, in echolalia, in fungi, in bacteria. LOX 5, LOX 8, LOX 12 and LOX 15, the four-headed isoenzymes of LOX enzymes are commonly found in animal tissues. In this study, LOX enzyme from bovine liver was partially purified by precipitation of ammonium sulphate at 30-50% saturation. Characterization studies were carried out and the optimum ionic strength value was determined as 0.5 mM, optimum pH value was pH 4.0 and optimum temperature value was 30 °C. The inhibitory effect of salicylic acid, eupatorin, eupatilin and gardenin A on LOX enzyme was investigated. Inhibitory effect of salicylic acid, eupatorin, eupatilin and gardenin A on LOX enzyme was investigated. IC50 values were calculated as 1.43 μM for salicylic acid, 0.46 μM for eupatorin, 0.15 μM for eupatilin and 5.31 μM for gardenin A.