Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9954165 | International Journal of Biological Macromolecules | 2018 | 20 Pages |
Abstract
The glutathione S-transferase (GST) was purified from fresh blood erythrocytes using affinity column chromatography. Also, α-amylase from porcine pancreas and α-glycosidase from Saccharomyces cerevisiae were used as target enzymes. In this study, these compounds were tested on α-amylase, α-glycosidase, and GST enzymes and demonstrated effective inhibitor compounds with Ki values in the range of 8.34-40.78â¯Î¼M against GST, and 120.53-892.36â¯nM against α-glycosidase. Additionally, the phenolic molecules were tested for the inhibition of α-amylase enzyme which determined effective inhibition profile with IC50 values in the range of 175.01-626.58â¯nM. Indeed, these molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents.
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Authors
İlhami Gulçin, Parham Taslimi, AyÅenur Aygün, Nastaran Sadeghian, Enes Bastem, Omer Irfan Kufrevioglu, Fikret Turkan, Fatih Åen,