A novel fibrinolytic enzyme, ACase was isolated from fruiting bodies of a mushroom, Agrocybe aegerita. ACase was purified by using ammonium sulfate precipitation, gel filtration, ion exchange and hydrophobic chromatographies to 237.12 fold with a specific activity of 1716.77 U/mg. ACase was found to be a heterodimer with molecular mass of 31.4 and 21.2 kDa by SDS-PAGE and appeared as a single band on Native-PAGE and fibrin-zymogram. The N-terminal sequence of the two subunits of ACase was AIVTQTNAPWGL (subunit 1) and SNADGNGHGTHV (subunit 2). ACase had maximal activity at 47 °C and pH 7.6. It's activity was improved by Cu²⁺, Na⁺, Fe³⁺, Zn²⁺, Ba²⁺, K⁺ and Mn²⁺, but inhibited by Fe²⁺, Mg²⁺ and Ca²⁺. PMSF, SBTI, aprotinine and Lys inhibited the enzyme activity, which suggested that ACase was a serine protease. ACase could degrade all three chains (α, β and γ) of fibrinogen. Moreover, the enzyme acted as both, a plasmin-like fibrinolytic enzyme and a plasminogen activator. It could hydrolyze human thrombin slightly, which indicated that the ACase could inhibit the activity of thrombin and acted as an anticoagulant to prevent thrombosis. Based on these results, ACase might act as a therapeutic agent for treating thrombosis, or as a functional food. Further investigation of the enzyme is underway.

从蘑菇菇（Agrocybe aegerita）的子实体中分离出一种新型的纤溶酶ACase 。通过使用硫酸铵沉淀，凝胶过滤，离子交换和疏水色谱法将ACase纯化至237.12倍，比活性为1716.77 U / mg。通过SDS-PAGE发现ACase是分子量为31.4和21.2kDa的异二聚体，并且在Native-PAGE和纤维蛋白酶谱图上显示为单条带。ACase的两个亚基的N端序列是AIVTQTNAPWGL（亚基1）和SNADGNGHGTHV（亚基2）。ACase在47°C和pH 7.6下具有最大活性。Cu 2 ⁺，Na ⁺，Fe ³⁺，Zn 2 ⁺，Ba 2 ⁺，K改善了它的活性⁺和Mn ²⁺，但受Fe 2 ⁺，Mg ²⁺和Ca ²⁺抑制。PMSF，SBTI，抑肽酶和Lys抑制了酶的活性，这表明ACase是一种丝氨酸蛋白酶。ACase可以降解纤维蛋白原的所有三个链（α，β和γ）。此外，该酶同时充当纤溶酶样纤溶酶和纤溶酶原激活剂。它可以使人的凝血酶轻微水解，表明ACase可以抑制凝血酶的活性，并起着抗凝剂的作用，可以防止血栓形成。基于这些结果，ACase可能充当血栓形成的治疗剂或功能性食品。该酶的进一步研究正在进行中。