INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, cilt.119, ss.741-746, 2018 (SCI-Expanded)
The glutathione S-transferase (GST) was purified from fresh blood erythrocytes using affinity column chromatography. Also, alpha-amylase from porcine pancreas and alpha-glycosidase from Saccharomyces cerevisiae were used as target enzymes. In this study, these compounds were tested on alpha-amylase, alpha-glycosidase, and GST enzymes and demonstrated effective inhibitor compounds with K-i values in the range of 8.34-40.78 mu M against GST, and 120.53-892.36 nM against alpha-glycosidase. Additionally, the phenolic molecules were tested for the inhibition of alpha-amylase enzyme which determined effective inhibition profile with IC50 values in the range of 175.01-626.58 nM. Indeed, these molecules can be elective inhibitors of GST, alpha-glycosidase and alpha-amylase enzymes as antidiabetic and antiparasitic agents. (C) 2018 Elsevier B.V. All rights reserved.