The effects of norepinephrine on lactoperoxidase enzyme (LPO)

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

SCIENTIFIC RESEARCH AND ESSAYS, cilt.5, sa.11, ss.1351-1356, 2010 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 5 Sayı: 11
  • Basım Tarihi: 2010
  • Dergi Adı: SCIENTIFIC RESEARCH AND ESSAYS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1351-1356
  • Anahtar Kelimeler: Noradrenaline, norepinephrine, lactoperoxidase, LPO, enzyme purification, inhibition, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, CHIONANTHUS-VIRGINICUS L., STRUCTURE-ACTIVITY INSIGHT, BRASSICA-OLERACEA L., CARBONIC-ANHYDRASE, ANTIOXIDANT ACTIVITY, BOVINE LACTOPEROXIDASE, ANTIRADICAL ACTIVITIES, LIPID-PEROXIDATION
  • Atatürk Üniversitesi Adresli: Evet

Özet

Norepinephrine, a hormone and a neurotransmitter, was known as catecholamine. In the present study, we examined the inhibitory effect of norepinephrine on lactoperoxidase enzyme purified from bovine milk. Lactoperoxidase (LPO; E.C.1.11.1.7) was purified from bovine milk with three purification steps: Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange chromatography and Sephadex G-100 gel filtration chromatography, respectively. LPO was purified with a yield of 31.5%, a specific activity of 30.33 EU/mg proteins and 20.77 purification fold. To determine enzyme purity, SDS-PAGE was performed and single band was observed. The R-z (A(412)/A(280)) value for LPO was 0.9. The effect of norepinephrine on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC50) value norepinephrine was found to be 67.2 mu M. Also, inhibition constant (K-i) for norepinephrine was found to be 62.0 mu M. Norepinephrine was found as noncompetitive inhibitor.