The inhibition effects of some natural products on lactoperoxidase purified from bovine milk. Issue 9 (8th June 2017)

• Record Type: Journal Article
• Authors: Köksal, Zeynep; Kalın, Ramazan; Gerni, Serpil; Gülçin, İlhami; Özdemir, Hasan
• Is Part Of: Journal of biochemical and molecular toxicology. Volume 31:Issue 9(2017)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-06-08
• Subjects: enzyme inhibition -- enzyme purification -- lactoperoxidase -- natural products -- phenolic compounds; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Toxicology -- Periodicals; 574
• DOI: 10.1002/jbt.21939
• Languages: English
• ISSNs: 1095-6670

Abstract

Abstract: In this study, inhibition profiles of some natural products, which are digoxin, L‐Dopa, dopamine, isoliquiritigenin, and 1, 1, 2, 2‐tetrakis( p ‐hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme. Digoxin, L‐Dopa, and dopamine are active ingredients of some drugs, which have important functions in our body, especially in cases of heart failure. Isoliquiritigenin and tetrakis are types of natural phenolic compounds, which play an important role in cancer prevention and treatment. LPO enzyme was purified from bovine milk using sepharose‐4B‐l ‐tyrosine sulfonamide affinity column chromatography. LPO is responsible for the nonimmune biological defense system and has antibacterial activity so selection of these active substances is important. The inhibition studies are performed with the ABTS substrate. Bovine LPO enzyme was effectively inhibited by phenolic molecules. Ki values of these natural products were found as 0.20 ± 0.09, 0.22 ± 0.17, 0.49 ± 0.11, 0.49 ± 0.27, and 1.20 ± 0.25 μM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.