Purification of glutathione<i>S</i>-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities

Demirdağ, Ramazan; Yerlikaya, Emrah; Küfrevioğlu, Ömer İrfan; Gündoğdu, Cemal

doi:10.3109/14756366.2012.694878

Cited by 5 publications

(3 citation statements)

References 31 publications

(29 reference statements)

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“…In our this study in vitro inhibition rank order was determined also as Se 2+ > B 3+ > Ag + > Al 3+ Ba 2+ > Cd 2+ > Pb 2+ > Ni 2+ > Fe 3+ > Cu 2+ > Zn 2+ > Co 2+ . The results obtained in our work are similar to data reported by many researchers [3,5,7,[17][18][19][20]22]. In recent years, people have become concerned about the water, soil and air pollution by various heavy metals.…”

Section: Discussionsupporting

confidence: 91%

Carbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver : Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicity

Yerlikaya

Karageçili²,

Demirdağ³

et al. 2017

HJBC

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F izyolojik ve klinik özelliklerinden dolayı karbonik anhidrazlar (CAs), en çok incelenen enzimlerdir. Daha önceki çalışmalarda CA enzimleri köpek, domuz, koyun, tavuk, arı, balık, sığır, bakteri ve insan gibi birçok canlının dokularından ve eritrositlerinden saflaştırılmış ve karakterize edilmiştir. Bu çalışmada da CA enzimi Siirt Tiftik Keçisi karaciğer dokusundan 1930.84 EU.mg -1 spesifik aktivite ile %57.28 verimle 80.55 kat saflaştırıldı. Saflaştırılan enzimin saflığı SDS-PAGE ile doğrulandı. Siirt Tiftik Keçisi karaciğerinden CA enziminin karakterizasyonu yapıldığında; optimum iyonik şiddet: 25 mM, optimum pH: 8.0, optimum sıcaklık: 40ºC ve stabil pH: 7.0 olarak belirlendi. Saflaştırılmış CA enzimi üzerine bazı metal iyonlarının inhibitör etkileri incelendi. İnhibisyon gösteren metal iyonlarının IC 50 değerleri

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Section: Discussionsupporting

confidence: 91%

Carbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver : Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicity

Yerlikaya

Karageçili²,

Demirdağ³

et al. 2017

HJBC

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“…The baths in which the activity measurement was performed were thoroughly mixed by adding 200 μl of 0.1 M (K 2 HPO 4 /KH 2 PO 4 pH: 7.0) 25 mM 20 μl of 95% CDNB (in ethanol) and 20 mM 50 μl GSH. After 20 μl enzyme sample was added rapidly, the sample was placed into the spectrophotometer with a cuvette and the absorbance values were measured for 3 minutes [36].…”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of glutathione S-transferase from blueberry fruits (Vaccinium arctostaphylos L.) and investigated of some pesticide inhibition effects on enzyme activity

Balcı

Türkan

Şakiroğlu

et al. 2019

Heliyon

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Pesticides cause pollution by remaining in water, soil, fruits and vegetables for a long time and also reach human through the food chain. It was thought that some pesticides used in agriculture could adversely affect the antioxidant enzyme system and the minimum inhibition values were studied. glutathione s-transferase (GST), an important antioxidant enzyme, catalyzes the conjugation of glutathione with toxic metabolites. It was purified from the blueberry fruits. The purification of the enzyme was performed separately by affinity and gel filtration chromatography. The purity of the enzyme was determined by SDS-PAGE electrophoresis. Characterization studies were done for the enzyme. For this purpose, optimal pH, temperature, K m and V max values for GSH and CDNB were also determined for the enzyme as 7.2 in K-phosphate buffer, 50 °C, 1.0 M, 7.0 in K-phosphate buffer, 1.57 mM; 0.17 mM and 0.048 EU/mL, 0.0159 EU/mL, respectively. Additionally, inhibitory effects of some pesticides; dichlorvos, acetamiprid, cyhalothrin, haloxyfop-p-Methyl, 2,4 dichlorophenoxy acetic acid, cypermethrin, imidacloprid, fenoxaprop-p-ethyl, glyphosate isopropylamine salt were examined the enzyme activity in vitro by performing Lineweaver–Burk graphs and plotting activity % IC 50 and K i values were calculated for each of pesticides. All of the pesticides inhibited the GST enzyme at millimolar level. Pesticide showing the best inhibitory effect was found as dichlorvos. The Ki value which is the inhibition constant of this pesticide was 0.0175 ± 0.005.

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“…In this GST the bound is washed with buffer (50 mM Tris-HCI buffer pH 9.0 and up to 10 mM GSH) and eluted fractions in 2 mL volume were collected. The active fractions were separated and this fractions stored at +4 °C for the protein and enzyme activity measured (Demirdağ et al, 2012).…”

Section: Purification Of Gst Enzymementioning

confidence: 99%

Glutatyon S-Transferaz Enzim Aktivitesi Üzerine Amoksilin ve Vankomisin Hidroklorid Hidratın Etkisi: Bir in vitro çalışma

Türkan¹,

Atalar²

2018

Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi

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Glutathione S-transferase (GST) enzymes detoxify a broad spectrum of xenobiotics, including chemotherapeutic drugs, environmental carcinogens, and endogenous molecules. Glutathione transferases catalyze the conversion of some metabolites into less toxic substances. Phase II reactions, which often result in detoxification, are conjugation reactions of glutathione through GST enzymes that protect the organism from the attacks of highly reactive electrophilic substances. Since the GST enzyme can metabolize toxic exogenous compounds, it has been extensively investigated in mammals. In this study, the GST enzyme was purified in human erythrocytes with a specific activity of 5.56 EU mg -1 protein and a yield of 2316.0 fold with 65% efficienc. SDS-polyacrylamide gel electrophoresis was performed to check the purity of the purified enzyme and the molecular mass was determined to be about 26 kDa. The IC 50 and Ki values for amoxycillin and vancomycin hydrochloride drugs on the purified GST enzyme were calculated and the type of inhibition was determined. As a result of the inhibition studies, we observed that these antibiotics inhibited the GST enzyme at low doses.

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Purification of glutathioneS-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities

Cited by 5 publications

References 31 publications

Carbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver : Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicity

Carbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver : Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicity

Purification and characterization of glutathione S-transferase from blueberry fruits (Vaccinium arctostaphylos L.) and investigated of some pesticide inhibition effects on enzyme activity

Glutatyon S-Transferaz Enzim Aktivitesi Üzerine Amoksilin ve Vankomisin Hidroklorid Hidratın Etkisi: Bir in vitro çalışma

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