Arreguín R, Arreguín B, Soriano-García M, Hernández-Arana A, Rodríguez-Romero A
Instituto de Química, Universidad Nacional Autónoma de México, D.F.
FEBS Lett. 1993 Apr 12;320(3):235-8. doi: 10.1016/0014-5793(93)80593-j.
A protein that showed activity against proteic (casein and hide powder azure) and synthetic (BAEE and HLPA) substrates was isolated from the marine sponge Spheciospongia vesparia. The protease was purified from an aqueous extract by ammonium sulfate precipitation, gel filtration, hydrophobic and HPLC-anion exchange chromatographies. The purified protease showed a single band in SDS-PAGE minigels and had a molecular weight of 29,600, but when submitted to isoelectric focusing it showed 2 bands with isoelectric points of 4.56 and 4.43. Its catalytic action was inhibited by EDTA and 1,10-phenanthroline, so it seemed to be a metalloprotease.
从海洋海绵黄球海绵（Spheciospongia vesparia）中分离出一种对蛋白质底物（酪蛋白和皮粉天青）以及合成底物（苯甲酰-L-精氨酸乙酯和L-亮氨酸对硝基苯胺）具有活性的蛋白质。该蛋白酶通过硫酸铵沉淀、凝胶过滤、疏水色谱和HPLC阴离子交换色谱从水提取物中纯化得到。纯化后的蛋白酶在SDS-PAGE小型凝胶中显示出一条带，分子量为29,600，但在进行等电聚焦时显示出两条带，等电点分别为4.56和4.43。其催化作用受到EDTA和1,10-菲啰啉的抑制，因此它似乎是一种金属蛋白酶。
