Ataturk University, Science Faculty, Department of Chemistry, Erzurum, Turkey.
J Enzyme Inhib Med Chem. 2012 Dec;27(6):795-9. doi: 10.3109/14756366.2011.615744. Epub 2011 Oct 10.
In this study; sheep carbonic anhydrase-II (SCA-II) (E.C: 4.2.1.1) was purified from sheep liver and in vitro effects of heavy metals on the enzyme was examined. SCA-II isozyme was purified with about 203 purification fold, a specific activity of 2320 EU/mg-protein and a yield of 72 by using Sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. Purity of the SCA-II enzyme was verified by SDS-PAGE technique and subunit molecular mass of the enzyme was found as 29 kDa. In addition to this, inhibitory effects of some metal ions on the enzyme were examined. In this study, sheep liver tissue was chosen; because the liver is an organ in which metal wastes of air, water and food are collected and it is easy to obtain the liver tissue. Because of the very important duties of CA enzyme on living beings, the effect of metals on the CA enzyme was investigated.
在这项研究中，从绵羊肝脏中纯化了绵羊碳酸酐酶-II（SCA-II）（EC：4.2.1.1），并研究了重金属对该酶的体外影响。使用 Sepharose-4B-L 酪氨酸磺酰苯胺亲和凝胶层析法，将 SCA-II 同工酶纯化约 203 倍，比活为 2320 EU/mg 蛋白，产率为 72%。SDS-PAGE 技术验证了 SCA-II 酶的纯度，并且发现酶的亚基分子量为 29 kDa。此外，还研究了一些金属离子对该酶的抑制作用。在这项研究中，选择绵羊肝脏组织，是因为肝脏是空气、水和食物中金属废物的收集器官，并且很容易获得肝脏组织。由于 CA 酶在生物体内具有非常重要的作用，因此研究了金属对 CA 酶的影响。
