Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds

Erol, Kadir; Gençer, Nahit; Arslan, Mikail; Arslan, Oktay

doi:10.3109/10731199.2012.696065

Cited by 11 publications

(5 citation statements)

References 20 publications

(16 reference statements)

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“…A 37-fold purification with a yield of 1.127% was found 29 . PON was purified and characterized from the Merino and Kivircik sheep's blood serums by a two-step procedure using ammonium sulfate precipitation and Sepharose-4B-L-tyrosine-1-napthylamine hydrophobic interaction chromatography for the first time by Erol et al On SDS polyacyrilamide gel electrophoresis, purified human serum paraoxonase yielded a single band of 66 kDa on SDS-PAGE 30 . Figure 3 illustrates the final purification patterns determined by SDS gel electrophoresis.…”

Section: Resultsmentioning

confidence: 99%

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

Demir

Gençer

Arslan

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this study, an alternative purification method for human paraoxonase 1 (hPON1) enzyme was developed using two-step procedures, namely, ammonium sulfate precipitation and Sepharose-4B-L-tyrosine-3-aminophenantrene hydrophobic interaction chromatography. SDS-polyacrylamide gel electrophoresis of the enzyme indicates a single band with an apparent M(W) of 43 kDa. The enzyme was purified 219-fold with a final specific activity of 4,408,400 U/mg and a yield of 10%. Furthermore, we examined the in vitro effects of some anabolic compounds, such as zeranol, 17 β-estradiol, diethylstilbestrol, oxytocin, and trenbolone on the enzyme activity to understand the better inhibitory properties of these molecules. The five anabolic compounds dose dependently decreased the activity of hPON1 with inhibition constants in the millimolar-micromolar range. The results show that these compounds exhibit inhibitory effects on hPON1 at low concentrations with IC50 values ranging from 0.064 to 16.900 µM.

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Section: Resultsmentioning

confidence: 99%

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

Demir

Gençer

Arslan

2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…In summary, enzyme inhibition is an important issue for drug design and biochemical applications [41][42][43][44][45]. Our results suggest that these novel compounds are likely to be adopted as candidates for the treatment of glaucoma and that they should be further evaluated in in vivo studies.…”

Section: T a B L Ementioning

confidence: 88%

In vitro inhibition of purified human carbonic anhydrase I and II by novel fluorene derivatives

Demirhan

Arslan

Kaya

et al. 2014

Maced. J. Chem. Chem. Eng.

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In this study, 9-benzylidene-9H-fluorene-substituted urea (5a-p) and thiourea derivatives (5q-v) were synthesized and their inhibitory effects on the activity of human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II were purified from human erythrocytes using a Sepharose 4B-L-tyrosinesulphanilamide affinity column. All the synthesized compounds inhibited the activity of the hCA I and II isoenzymes. Among the synthesized compounds, 5f was found to be the most active (IC 50 = 21.4 μM) for inhibition of hCA I and 5s was the most active (IC 50 = 25.3 μM) for inhibition of hCA II. IN VITRO ИНХИБИЦИЈА НА ПРЕЧИСТЕНА ЧОВЕЧКА КАРБОНСКА АНХИДРАЗА I И II СО НОВИ ФЛУОРЕНСКИ ДЕРИВАТИВо оваа студија беа синтетизирани деривати на уреа (5a-p) и тиоуреа (5q-v) добиени со супституција на 9-безилиден-9H-флуорен и беше проценет нивниот инхибиторен ефект врз човечка карбонска анхидраза (hCA) I и II. HCA I и II беа пречистени од човечки еритроцити со употреба на афинитетната колона Sepharose 4B-L-тирозин-сулфаниламид. Сите синтетизирани соединенија ја инхибираа активноста на изоензимите на hCA I и II. Од синтетизираните соединенија, 5f се покажа најактивно (IC 50 = 21,4 μM) за инхибиција на hCA I, додека 5s беше најактивно (IC 50 = 25,3 μM) за инхибиција на hCA II.Клучни зборови: 9-безилиден-9H-флуорен; уреа; тиоуреа; карбонска анхидраза; инхибиција

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“…Therefore, it is seen that Cu and Zn heavy metal ions affect PON enzyme activity studied in bonito (S. sarda) fish, similar to that of human PON1 enzyme and PON1 enzyme activity purified from bull semen. Erol et al (2013), in another study, examined the effect of some metal ions on PON1 enzyme activity purified from blood samples taken from Merino and Kivircik sheep breeds. It was determined that Mn +2 , Hg +2 , Co +2 , Cd +2 , Ni +2, and Cu +2 metal ions showed different levels of inhibition effect on PON enzyme activity and Cu +2 heavy metal ion caused strongest inhibitor effect for PON (Erol et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

“…Erol et al (2013), in another study, examined the effect of some metal ions on PON1 enzyme activity purified from blood samples taken from Merino and Kivircik sheep breeds. It was determined that Mn +2 , Hg +2 , Co +2 , Cd +2 , Ni +2, and Cu +2 metal ions showed different levels of inhibition effect on PON enzyme activity and Cu +2 heavy metal ion caused strongest inhibitor effect for PON (Erol et al, 2013). When examined the effects of heavy metal ions used in this study on PON enzyme activity in bonito (S. sarda) fish, it is seen that Cu +2 metal ion caused a partial decrease in the enzyme activity compared to other heavy metal ions (Hg +2 , Zn +2 ) used in the study.…”

Section: Discussionmentioning

confidence: 99%

The effect of mercury, copper, and zinc on paraoxonase (PON) enzyme activity in Bonito (Sarda sarda) fish

Şahin¹,

Çenesiz²

2021

EgeJFAS

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Since heavy metal dirtiness, which we frequently encounter in environmental pollution causes harmful effects on the organism through biochemical enzyme reactions, in this study, the effects of mercury (Hg+2), copper (Cu+2), and zinc (Zn+2) heavy metal ions, which are common in environmental pollution, on PON (paraoxonase) enzyme activity in muscle tissue of bonito (Sarda sarda) were investigated. In the study, 25 bonito (S. sarda) fish muscle tissues freshly obtained from the Samsun region sea were used. The changes in PON enzyme activity were determined by adding different volumes of heavy metal solutions. PON enzyme activities of Hg+2 heavy metal ion used in different volumes were calculated as 30.9383 U/mLdak, 29.0598 U/mLdak, 26.3799 U/mLdak, 23.9443 U/mLdak, 20.6725 U/mLdak, PON enzyme activities of Cu+2 heavy metal ion used in different volumes were calculated as 19.7949 U/mLdak, 19.4807 U/mLdak 19.1864 U/mLdak, 19.1200 U/mLdak, 18.9037 U/mLdak and PON enzyme activities of Zn+2 heavy metal ion used in different volumes were calculated as 23.8305 U/mLdak, 23.0781 U/mLdak, 22.9073 U/mLdak, 22.4324 U/mLdak, 21.8159 U/mLdak. As a result of these obtained data, activity (%) values were calculated and activity (%) graphs were drawn. As a result of the study, it was determined that increasing concentrations of Cu+2 and Zn+2 heavy metal ions caused a decrease in PON enzyme activity, but there was no statistically significant difference between the different concentrations used. It was determined that increasing concentrations of Hg+2 heavy metal ion inhibited the PON enzyme activity, caused a statistically significant decrease between the activities depending on the different concentrations used (p < 0.05).

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Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds

Cited by 11 publications

References 20 publications

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

In vitro inhibition of purified human carbonic anhydrase I and II by novel fluorene derivatives

The effect of mercury, copper, and zinc on paraoxonase (PON) enzyme activity in Bonito (Sarda sarda) fish

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