Effects of some anti-neoplastic drugs on sheep liver sorbitol dehydrogenase

Alım, Zuhal; Beydemır, Şükrü

doi:10.3109/13813455.2012.688055

Cited by 26 publications

(30 citation statements)

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“…That is why enzyme inhibition studies are an important issue for drug design and biochemical applications (Alim & Beydemir, 2012;Demir et al, 2012a, b;Sayin et al, 2012;Sonmez et al, 2011). This study is the first report on the inhibition of cytosolic carbonic anhydrases by various antipsychotic drugs.…”

Section: Resultsmentioning

confidence: 82%

Antipsychotic agents screened as human carbonic anhydrase I and II inhibitors

Erzengin

Bilen

Ergün

et al. 2013

Archives of Physiology and Biochemistry

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The antipsychotic drugs currently used to treat schizophrenia can be divided into two distinct classes, typical and atypical antipsychotics. Many drug molecules are enzyme inhibitors that bind reversibly or irreversibly to their target through intermolecular interactions. That's why enzyme inhibition studies are an important issue for drug design and biochemical applications. In this study, in vitro inhibition effect of some antipsychotic drugs on the purified carbonic anhydrase (CA) I and II isoenzymes were investigated by using CO2 as a substrate. CA I and II were purified from human erythrocytes by a simple one step procedure using Sepharose 4B-L-tyrosine-sulfonamide affinity column. The results showed that all the drugs inhibited the cytosolic carbonic anhydrases enzyme activity in a concentration-dependent fashion. Among the studied drugs, aripiprazole and pramipexole were found to be the most active one for hCA I (IC50: 3.64 and 5.37 μM) and hCA II (IC50: 4.16 and 4.81 μM) activity, respectively.

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Section: Resultsmentioning

confidence: 82%

Antipsychotic agents screened as human carbonic anhydrase I and II inhibitors

Erzengin

Bilen

Ergün

et al. 2013

Archives of Physiology and Biochemistry

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“…These enzymes have been purified from different tissues. Drug interactions studies of these essential enzymes have made significant contributions to the academic literature in the field of drug metabolism . For instance, we purified PON1 enzyme from human serum by using chromatographic methods.…”

Section: Discussionmentioning

confidence: 99%

A potential risk factor for paraoxonase 1: in silico and in-vitro analysis of the biological activity of proton-pump inhibitors

Türkeş

2019

Journal of Pharmacy and Pharmacology

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Objectives Proton‐pump inhibitors (PPIs) are drugs commonly utilized by about 7% of adults in the world. Recent researches have shown that there are countless and severe side effects of these drugs. This situation has raised concern among clinicians and patients alike. The purpose of this study is to contribute the novel drug discovery and development technology and toxicology field by researching interactions of PPIs on paraoxonase 1. Methods In this study, the paraoxonase 1 enzyme was purified from human serum by using rapid and straightforward chromatographic techniques. Subsequently, the inhibition effects of pantoprazole, omeprazole, and esomeprazole, PPIs, were investigated on paraoxonase 1. Besides, molecular docking studies were performed to unravel the binding mechanism between the enzyme and drugs. Key findings All drugs showed potent inhibitory activities. IC50 of the drugs values were 54.780 ± 0.524, 86.470 ± 0.818 and 93.390 ± 0.885 mm and Ki constants were found as 39.895 ± 0.005 mm, 70.112 ± 0.010 mm and 78.868 ± 0.008 mm, respectively. The binding scores observed in silico studies were found to agree with the obtained from in‐vitro experimental results. Conclusions We observed that the drugs decreased PON1 activity at low concentrations. The results show that adjusting the dosages of these medications is a crucial case for each patient. The physicians should more carefully interpret whether there is an essential indication before prescribing PPIs and, if there is, to approve the proper dosing for the situation.

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“…It is interesting that they found CA inhibition in in vivo. On the other hand, CA activity is inhibited at low concentrations in vitro conditions, at high concentrations are also activated Besides, paraoxonase, glucose-6-phosphate dehydrogenase and sorbitol dehydrogenase are enzymes studied the interactions with different chemicals Beydemir et al, 2003;Alım and Beydemir, 2012) In the present study, gentamycin, kanamycin, amikacin, lincomycin and clindamycin were selected to investigate inhibitory effect on the alcohol dehydrogenase activity. While the gentamycin, kanamycin and amikacin were aminoglycoside drugs, lincomycin and clindamycin were lincosamide group.…”

Section: Discussionmentioning

confidence: 99%

Alcohol Dehydrogenase from Sheep Liver: Purification, Characterization and Impacts of Some Antibiotics

Demir¹,

Şengül²,

Erğun³

et al. 2017

jist

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Alcohol dehydrogenase (ADH) is a dimeric enzyme in which each subunit of the enzyme has a Zn 2+ metal-containing catalytic domain and a cofactor-binding domain. This enzyme converts the alcohol to aldehyde. The present article focuses on the purification, characterization and in vitro effects of some antibiotics on alcohol dehydrogenase from sheep liver. ADH was purified with specific activity of 0.5 U/mg proteins and approximately 52.03-fold from sheep liver by DEAE-Sephadex A-50 ion exchange chromatography and gel filtration on Sephadex G-100. The subunit and the natural molecular weights of the enzyme were determined by gel filtration and SDS-PAGE 80.49 and 38.16 kDa, respectively. The optimum ionic strenght, temperature and, pH of ADH was 400 mM, 40°C and, 10.5, respectively. The inhibitory effects of the antibiotics were tested at various concentrations. IC 50 values for kanamycin sulfate, amikacin sulfate, gentamicin, lincomycin, and clindamycin were found to be 43. 31, 36.47, 20.38, 18.73 and 1.31 mM, respectively.

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Effects of some anti-neoplastic drugs on sheep liver sorbitol dehydrogenase

Cited by 26 publications

References 50 publications

Antipsychotic agents screened as human carbonic anhydrase I and II inhibitors

Antipsychotic agents screened as human carbonic anhydrase I and II inhibitors

A potential risk factor for paraoxonase 1: in silico and in-vitro analysis of the biological activity of proton-pump inhibitors

Alcohol Dehydrogenase from Sheep Liver: Purification, Characterization and Impacts of Some Antibiotics

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