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金属离子对凡纳对虾N-乙酰-β-D-氨基葡萄糖苷酶活力的影响 被引量:9

Effects of metal ions on activity of N-acetyl-β-D-glucosaminidase from prawn (Penaeus vannamei)
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摘要 本文报道了金属离子对凡纳对虾N-乙酰-β-D-氨基葡萄糖苷酶 (EC3. 2. 1. 52)活力的影响.结果表明,Li+、Na+和K+等对该酶活力没有任何效应.Ca2+、Mg2+、Mn2+对该酶有激活作用,而Ba2+、Al3+、Fe3+、Zn2+、Co2+、Cd2+、Hg2+、Pb2+和Cu2+对该酶活力均具有一定的抑制作用.以Hg2+的抑制作用最显著,Hg2+含量为 1. 5mmol/dm3 时可使酶活力完全丧失.进一步研究Zn2+的抑制作用动力学,结果表明:Zn2+对该酶的抑制作用属可逆的非竞争性类型,抑制常数为11. 95mmol/dm3. A study on the effects of metal ions on N-aceyl-β-D-glucosaminidase (NAGase, EC3.2.1.30) from Penaeus vannamei is surveyed. Li^+, Na^+ and K^+ have no any effects on the enzyme activity. Ca^(2+), Mg^(2+) and Mn^(2+) activate the enzyme, but Ba^(2+), Al^(3+), Fe^(3+), Zn^(2+), Co^(2+), Cd^(2+), Hg^(2+), Pb^(2+) and Cu^(2+) inhibit the enzyme. The inhibitory effect of Hg^(2+) is the most potent. 1.5 mmol/dm^3 of Hg^(2+) lead to the enzyme complete inactivation. The inhibitory kinetics of Zn^(2+) on the enzyme is further studied. The result shows that Zn^(2+) is a reversible noncompetitive inhibitor of the enzyme, and the inhibition constants(K_I) was determined to be 11.95 mmol/dm^3.
出处 《台湾海峡》 CAS CSCD 北大核心 2005年第1期78-82,共5页 Journal of Oceanography In Taiwan Strait
基金 福建省青年科技人才创新项目(2004J054) 厦门大学细胞生物学与肿瘤细胞工程教育部重点实验室开发基金资助项目(2004105)
关键词 海洋生物 N-乙酰-Β-D-氨基葡萄糖苷酶 实验研究 凡纳对虾 金属离子 marine biology N-acetyl-β-D-glucosaminidase experimental research Penaeus vannamei metal ions inhibitory kinetics
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