高等学校化学学报 ›› 2001, Vol. 22 ›› Issue (12): 1979.

• 研究论文 • 上一篇    下一篇

重金属离子对猪胰α-淀粉酶活性影响的作用机理研究

洪法水, 王雪峰, 吴康, 沈颂东, 苏国兴, 潘新法   

  1. 苏州大学生命科学院生物科学系, 苏州 215006
  • 收稿日期:2000-12-27 出版日期:2001-12-24 发布日期:2001-12-24
  • 通讯作者: 洪法水(1960年出生),男,博士,教授,从事生物无机化学研究.E-nmail:hongfsh cn@sina.com E-mail:hongfsh cn@sina.com
  • 基金资助:

    苏州大学人才引进基金(批准号:XQ316011)资助

Mechanism of Heavy Metal Ions on α-Amylase Activity from Porcine Pancreas

HONG FaShui, WANG XueFeng, WU Kang, SHEN SongDong, SU GuoXing, PAN XinFa   

  1. Department of Biology Science, College of Life Science, Suzhou University, Suzhou 215006, China
  • Received:2000-12-27 Online:2001-12-24 Published:2001-12-24

摘要: 通过在α-淀粉酶介质中加入Ce3+,Cd2+和Pb2+,研究其对α-淀粉酶活性影响的作用机理.结果表明,低浓度重金属离子对酶活性有激活作用,高浓度则严重抑制酶活性.在高浓度下,Ce3+,Cd2+和Pb2+能完全竞争出α-淀粉酶中的Ca2+.荧光滴定结果表明,Ce3+,Cd2+和Pb2+不仅可能完全占据Ca2+的结合位点,而且还可能在Ca2+的结合位点以外的氨基酸残基上结合,从而导致酶的构象改变.

关键词: &alpha, -淀粉酶, 重金属离子, 酶活性, 结合位点

Abstract: The activity of αamylase from porcine pancreas was enhanced under the treatment by Ce3+, Cd2+ and Pb2+ at a low concentration (0.5-5 μmol/L) , but was inhibited by Ce3+, Cd2+ and Pb2+ at a high concentration(4 or 5 μmol/Labove). Ce3+, Cd2+ and Pb2+ at a high concentration could competitively displace Ca2+ from αamylase. The equilibrium dialysis demonstrated that αamylase have five Ca2+binding sites with different affinities. The fluorescence titration showed that Ce3+, Cd2+ and Pb2+ are not only bound to Ca2+binding sites, but also bound to other sites of αamylase, and resulted in the αamylase conformational changes.

Key words: Amylase, Heavy metal ions, Enzyme activity, Binding site

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