Purification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities. (1st October 2013)

• Record Type: Journal Article
• Authors: Demirdag, Ramazan; Yerlikaya, Emrah; Kufrevioglu, Omer Irfan; Gundogdu, Cemal
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 28:Number 5(2013:Oct.)
• Page Start: 911
• Page End: 915
• Publication Date: 2013-10-01
• Subjects: Cancer -- GST -- enzyme -- metal -- inhibition; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.3109/14756366.2012.694878
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract : 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. Mg 2+ and Cd 2+ had inhibitory effect on the enzymes activities. Other kinetic properties of the enzymes were also determined.