Research Information System
Thesis Type: Postgraduate
Institution Of The Thesis: Erzincan Binali Yildirim University, Eczacılık Fakültesi, Temel Eczacılık Bilimleri Bölümü, Turkey
Approval Date: 2021
Thesis Language: Turkish
Student: Ebru AKMAN
Supervisor: Esra Dilek
Abstract:
Introduction and Aim: Enzymes are biological catalysts that serve in all biochemical
reactions that make up the metabolism in living systems. Carbonic anhydrase (E.C.4.2.1.1)
was obtained from human erythrocytes, while acetylcholine esterase (AChE, acetylcholine
acetylhydrolase, EC 3.1.1.7) was readily obtained. As the first step of the study, its in vitro
effects on carbonic anhydrase isoenzyme I and II (hCA-I and hCA-II) were investigated.
Material and Method: First, hCA-I and hCA-II isoenzymes were purified using Sepharose4B-L-Tyrosine-sulfinamide affinity column chromatography. To determine the purity of the
enzymes, SDS-PAGE was performed. After purification, the inhibition effects of indole
derivative Schiff base compounds on hCA-I and hCA-II enzoenzymes were examined and Ki
and IC50 values were calculated. In our study, the inhibitory effects of indole-derived schiff
base compounds on AChE activity were also investigated. In the inhibition studies of AChE,
activity was measured according to the Ellman method. IC50 and Ki values were calculated for
each substance.
Results: In the study, IC50 and Ki values were determined to be in the range of 38.50-231.05
nM and 36.18 ± 3.07-224.29 ± 5.78 nM for hCA-I isoenzyme, respectively. The same
parameters were calculated in the range of 33.01-216.28 nM and 31.30 ± 2.63-201.64 ± 7.25
nM for the hCA-II isoenzyme. The IC50 and Ki values for AChE of indole derivative Schiff
base compounds were determined to be in the range of 31.84 - 135.90 nM and 6.82 ± 0.72 -
110.30 ± 9.26 nM.
Conclusions: It was observed that indole derivative Schiff base compounds inhibited hCA-I,
hCA-II and AChE enzymes significantly.