Purification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.28, sa.5, ss.911-915, 2013 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 28 Sayı: 5
- Basım Tarihi: 2013
- Doi Numarası: 10.3109/14756366.2012.694878
- Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.911-915
- Anahtar Kelimeler: Cancer, GST, enzyme, metal, inhibition, GASTRIC-CANCER, RAT, EXPRESSION, RESISTANCE, TISSUES, RISK
- Atatürk Üniversitesi Adresli: Evet
Özet
In this study, glutathione S-transferase (GST) enzyme was purified from nontumour and tumour human gastric tissue and in vitro effects of heavy metals on the enzyme were examined. GST was purified 3089 fold with a specific activity of 20 U/mg and a yield of 78% from gastric tumour tissue; and 1185 fold with a specific activity of 5.69 U/mg and a yield of 50% from nontumour tissue by using glutathione-agarose affinity column, respectively. Enzyme purity was verified by SDS-PAGE and subunit molecular mass was calculated around 26 kDa. The molecular weight of the enzyme was calculated as 52 kDa by using Sephadex G-75 gel filtration column. Then, inhibitory effects of metal ions on the enzymes were investigated. Mg2+ and Cd2+ had inhibitory effect on the enzymes activities. Other kinetic properties of the enzymes were also determined.