Abstract
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 Rz (A412/A280) 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 µM. Also, inhibition constant (Ki) for norepinephrine was found to be 62.0 µM. Norepinephrine was found as non-competitive inhibitor. Key words: Noradrenaline, norepinephrine, lactoperoxidase, LPO, enzyme purification, inhibition.
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