Tsymanovich S A, Nikandrov V N, Maksimova R A, Sharkova T S, Andreenko G V, Serebriakova T N
Vopr Med Khim. 1992 May-Jun;38(3):44-5.
A preparation exhibiting high fibrinolytic activity and ability to activate plasminogen was isolated from cultivation medium of Arthrobotrys longa. Homogeneous protein, obtained after gel filtration on Sephadex G-100, had molecular mass 28,600, pI-3.68-3.74, optimum activity at pH 6.0-9.0 and temperature optimum at 37 degrees. The enzyme proved to be serine proteinase as shown by analysis using inhibitors; it required thiol groups.
从长柄节丛孢菌的培养基中分离出一种具有高纤溶活性和激活纤溶酶原能力的制剂。经Sephadex G - 100凝胶过滤后得到的均一蛋白质,分子量为28,600,等电点为3.68 - 3.74,在pH 6.0 - 9.0时活性最佳,最适温度为37℃。用抑制剂分析表明该酶为丝氨酸蛋白酶;它需要巯基。