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《Spectroscopy and Spectral Analysis》 2003-03
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Study of the Effect of Pb ~(2+) on α-Amylase Activity by Spectroscopy

HONG Fa-shui College of Life Sciences, Suzhou University,Suzhou 215006,China  
The activity of α-amylase from porcine pancreas was enhanced under the treatment by Pb 2+ at low concentration (0.5-4 μmol·L -1),but was inhibited by Pb 2+ at high concentration (above 4 μmol·L -1).Pb 2+ at high concentration could competitively displace Ca 2+ from α-amylase. The EXAFS demonstrated that Pb 2+ was bound to the active site of α-amylase, the coordination atom was oxygen,the coordination number was 2, and the Pb-O bond length was 0.234 nm.Circular dichroism spectra showed that the secondary structure of trypsin was greatly changed by Pb 2+ at high concentration,as α-helix,β-turn and random coil contents decreased,while β-sheet, aromatic and disulfide bond contents increased. It was suggested that Pb 2+ was bound to result in an α-amylase conformational change, and the enzyme activity decreased.
【Fund】: 苏州大学人才引进基金资助项目
【CateGory Index】: O657.3
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