| Literature DB >> 30076927 |
İlhami Gulçin1, Parham Taslimi2, Ayşenur Aygün3, Nastaran Sadeghian1, Enes Bastem1, Omer Irfan Kufrevioglu1, Fikret Turkan4, Fatih Şen5.
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 8.34-40.78 μM against GST, and 120.53-892.36 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 175.01-626.58 nM. Indeed, these molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents.Entities:
Keywords: Antidiabetic; Antiparasitic; Enzyme inhibition; Glutathione S-transferase
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Year: 2018 PMID: 30076927 DOI: 10.1016/j.ijbiomac.2018.08.001
Source DB: PubMed Journal: Int J Biol Macromol ISSN: 0141-8130 Impact factor: 6.953