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海洋科学  2008 

牙鲆孵化酶的分离纯化及其部分生物化学性质研究

, PP. 44-50

Keywords: 牙鲆(Paralichthys,olivaceus),孵化酶,卵膜裂解活性,丝氨酸蛋白酶,金属蛋白酶

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Abstract:

利用凝胶过滤柱层析和阴离子交换柱层析技术,从牙鲆(Paralichthysolivaceus)胚胎孵化液中分离纯化出了大小约为34.8ku的牙鲆孵化酶。该酶卵膜裂解的最适反应温度为35℃,最适pH为7.0;对底物酪蛋白的米氏常数Km值为1.53mmol/L。该酶对丝氨酸蛋白酶和胰蛋白酶的特异性抑制剂非常敏感,而对其他蛋白酶抑制剂不敏感,表明该酶极可能是一种丝氨酸蛋白酶类型的胰蛋白酶。此外,该酶可浓度依赖性地被EDTA所抑制,被Cu2+所强烈抑制,被Ca2+和Mg2+所激活,对Zn2+则不敏感,表明该酶很可能是一种金属蛋白酶。

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