Inhibition effects of selected thiophene-2-sulfonamides on lactoperoxidase
1Department of Chemistry, Faculty of Engineering and Natural Sciences, Istanbul Medeniyet University, Istanbul, Turkey.
Abstract:
Lactoperoxidase (LPO, E.C.1.11.1.7) is a natural antibacterial agent which is secreted from salivary, mammary, and other mucosal glands. It is one of the crucial enzymes in biological systems, so protection of LPO activity is extremely important for the immune system. Within the scope of this study; in vitro effects of some thiophene-2-sulfonamide derivatives (1a-7a) on bovine milk LPO enzymatic activity were investigated. LPO was purified from the Sepharose-4B-L-tyrosine-5-amino-2-methylbenzenesulfonamide column prepared using affinity chromatography technique with a yield of 169.66 EU/mg specific activity in 452.44 times. As a result, 5-(2-thienylthio) thiophene-2-sulfonamide demonstrated the strongest inhibition impact among these compounds. This molecule has shown a competitive inhibition and it was determined that the IC50 value was 3.4 nM and the Ki value was 2 ± 0.6 nM.
More Related Videos
07:19A Modified Lean and Release Technique to Emphasize Response Inhibition and Action Selection in Reactive Balance
Published on: March 19, 2020
06:022-Methacryloyloxyethyl Phosphorylcholine Polymer Treatment of Complete Dentures to Inhibit Denture Plaque Deposition
Published on: December 26, 2016
Related Concept Videos
Amines to Sulfonamides: The Hinsberg Test
Generally, a primary amine reacts with the Hinsberg reagent to produce an N-substituted benzenesulfonamide. The electron-withdrawing sulfonyl...
Feedback Inhibition
Buffer Effectiveness
The buffer capacity is the amount of acid or base that can be added to a given volume...
Enzyme Inhibition
What is Natural Selection?
Antibiotic Selection
