THE INHIBITORY EFFECTS OF L-ADRENALINE ON LACTOPEROXIDASE ENZYME PURIFIED FROM BOVINE MILK

ŞİŞECİOĞLU M., GÜLÇİN İ., ÇANKAYA M., ÖZDEMİR H.

INTERNATIONAL JOURNAL OF FOOD PROPERTIES, cilt.15, sa.6, ss.1190-1199, 2012 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 15 Sayı: 6
  • Basım Tarihi: 2012
  • Doi Numarası: 10.1080/10942912.2010.511924
  • Dergi Adı: INTERNATIONAL JOURNAL OF FOOD PROPERTIES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1190-1199
  • Anahtar Kelimeler: L-Adrenaline, Lactoperoxidase, Enzyme purification, Inhibition, ERYTHROCYTES IN-VIVO, CARBONIC-ANHYDRASE, VITRO, ANTIOXIDANT, PURIFICATION, DANTROLENE, RAT, COMPLEXES, MELATONIN, KINETICS
  • Atatürk Üniversitesi Adresli: Evet

Özet

L-Adrenaline belongs to a group of compounds known as catecholamines, which play an important role in the regulation of the physiological process in living organisms. In the present study, the inhibitory effect of L-adrenaline on lactoperoxidase was examined. Lactoperoxidase (E.C.1.11.1.7) was purified from bovine milk with three consecutive steps: Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange, and Sephadex G-100 gel filtration chromatography. Lactoperoxidase was purified with a yield of 42.18%, a specific activity of 30.33 EU/mg proteins, and 20.77 purification fold. Enzyme purity was determined with SDS-PAGE, where a single band was observed. The R-z (A(412)/A(280)) value for lactoperoxidase was 0.9. The effect of L-adrenaline on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC50) value and an inhibition constant (K-i) values for L-adrenaline were 34.5 and 2.26 mu M, respectively. L-Adrenaline was found to be a non-competitive inhibitor.