| 白灵侧耳纤溶酶的纯化及酶学性质分析 |
| Purification and characteristics of a fibrinolytic enzyme from Pleurotus nebrodensis |
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| 中文关键词:食药用真菌，纤溶活性，酶学特性 |
| 英文关键词:edible and medicinal fungi, fibrinolytic activity, enzyme property |
| 基金项目:国家“863”计划（No. 2007AA021506）；江苏省高校自然科学重大基础研究（No. 08KJA350001） |
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| 中文摘要: |
| 白灵侧耳子实体浸提液经过硫酸铵沉淀、DEAE-Sepharose Fast Flow阴离子交换层析、凝胶过滤层析和羟基磷灰石色谱柱层析后，纯化得到一种纤溶酶。该酶在SDS-PAGE中显单条带，其分子量约为30kDa。该酶在45℃以下，pH6.5－10.0的范围内稳定，最适pH为8.0，最适温度为25℃。金属离子K+对该酶有明显的激活作用，Zn2+、Mg2+、Cu2+对酶有部分抑制作用。金属离子鳌合剂EDTA和丝氨酸蛋白酶抑制剂PMSF不抑制该酶活性，初步说明此酶既不是金属酶，也不是丝氨酸类蛋白酶。该酶既具有纤溶酶作用，又具有激活纤溶酶原的作用。 |
| 英文摘要: |
| A fibrinolytic enzyme was purified from Pleurotus nebrodensis fruit bodies by ammonium sulfate precipitation, DEAE-Sepharose Fast Flow anion exchange chromatography, Bio-gel P30 gel filtration and CHT Ceramic Hydroxyapatite chromatography. SDS-PAGE analysis of the purified protein showed only one band with molecular mass of 30kDa. The fibrinolytic enzyme was stable blow 45℃ and pH6.5－10.0. The optimal temperature was 25℃ and the optimal pH was 8.0. K+ ion enhanced the fibrinolytic activity, whereas Zn2+, Mg2+and Cu2+ partly inhibited the enzyme. EDTA and PMSF couldn’t inhibit fibrinolytic activity, indicating that the enzyme didn’t belong to metalloenzyme and serine protease group. The enzyme not only directly degraded fibrin clot, but also had the ability of converting pladminogen to plasmin. |
| 鞠秀云,曹成亮,蒋继宏. 白灵侧耳纤溶酶的纯化及酶学性质分析[J]. 菌物学报, 2010, 29(3): 403-408 |
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