Akademik Veri Yönetim Sistemi
3rd International Eurasian Conference on Science, Engineering and Technology (EurasianSciEnTech 2021), Ankara, Türkiye, 15 - 17 Aralık 2021, ss.945, (Özet Bildiri)
Glutamate dehydrogenase (GDH) enzyme is a very important and functional metabolic enzyme because it
participates in the energy metabolism of proteins and the synthesis of metabolites important for the organism.
The bidirectional nature of the reaction catalyzed by the GDH enzyme can be customized according to the
needs and function of the tissue in which the enzyme is located. GDH enzyme was purified from the liver of
rainbow trout (Oncorhynchus mykiss) by 2',5'-ADP Sepharose 4B affinity chromatography in one step. As a
result of this purification process, GDH enzyme was purified 171-fold with 5.38 U/mg protein specific activity.
The effects of some metal ions and vitamins on the activity of the purified GDH enzyme were investigated.
As a result of these experiments, it was found that metal ions Ag+
, Cu2+, Zn2+, Ni2+, Fe2+, Mn2+, Co2+, Mg2+
,
Fe3+, Cr3+ ions had inhibitory effect and Ca2+ and V4+ ions had an activator effect on the GDH enzyme. It has
been determined that Na+
and Li+ metal ions have no effect on the activity of the purified GDH enzyme.
Likewise, the effects of some vitamins on the activity of the purified GDH enzyme were examined, and as a
result of the experiments, it was determined that B1, B6, and U vitamins had an inhibitory effect and vitamin
B2 had an activator effect. B3 and C vitamins were found to have no effect on GDH activity. IC50 values of
metals and vitamins showing inhibition effect were determined, Lineweaver-Burk plots were drawn by
calculating the inhibition type and Ki values.