Magalhães Marta R, da Silva Nelson Jorge, Ulhoa Cirano J
Centro de Estudos e Pesquisas Biológicas, Departamento de Biologia, Universidade Católica de Goiás, 74.605-010, Goiânia, GO, Brazil.
Toxicon. 2008 May;51(6):1060-7. doi: 10.1016/j.toxicon.2008.01.008. Epub 2008 Feb 2.
Freshwater stingrays (Potamotrygon motoro) are known to cause human accidents through a sting located in its tail. In the State of Goiás, this accident happens especially during the fishing season of the Araguaia River. The P. motoro venom extracted from the sting presented hyaluronidase activity. The enzyme was purified by gel filtration on Sephacryl S-100 and ion-exchange chromatography on SP-Sepharose. A typical procedure provided 376.4-fold purification with a 2.94% yield. The molecular weight of the purified enzyme was 79 kDa as estimated by gel filtration on Sephacryl S-100. The K(m) and V(max) values for hyaluronidase, using hyaluronic acid as substrate, were 4.91 microg/ml and 2.02 U/min, respectively. The pH optimum for the enzyme was pH 4.2 and maximum activity was obtained at 40 degrees C. The hyaluronidase from P. motoro was shown to be heat instable, being stabilized by bovine albumin and DTT, and inhibited by Fe(2+), Mn(2+), Cu(2+) and heparin.
淡水黄貂鱼（Potamotrygon motoro）已知会通过其尾部的毒刺导致人类受伤。在戈亚斯州，这种事故尤其发生在阿拉瓜亚河的捕鱼季节。从毒刺中提取的P. motoro毒液具有透明质酸酶活性。该酶通过在Sephacryl S - 100上进行凝胶过滤和在SP - Sepharose上进行离子交换色谱法进行纯化。一个典型的程序提供了376.4倍的纯化，产率为2.94%。通过在Sephacryl S - 100上进行凝胶过滤估计，纯化酶的分子量为79 kDa。以透明质酸为底物时，透明质酸酶的K(m)和V(max)值分别为4.91微克/毫升和2.02单位/分钟。该酶的最适pH为4.2，在40℃时获得最大活性。P. motoro的透明质酸酶显示出热不稳定性，可被牛血清白蛋白和二硫苏糖醇稳定，并被Fe(2+)、Mn(2+)、Cu(2+)和肝素抑制。
