This work was supported by grants from the Research Foundation of Suzhou University “211 Project” (XQ316011).
分别研究了Pb2+、Cd2+和Ce3+对Ca(Ⅱ) α-淀粉酶活性影响及对其Ca2+的竞争作用.结果表明三种金属离子低浓度情况下(0.5~5 mmol/L)对α-淀粉酶具有激活现象,而较高浓度则抑制酶活力.Pb2+、Cd2+和Ce3+竞争置换α-淀粉酶中Ca2+能力的大小是:Pb2+>Cd2+>Ce3+,其抑制酶活作用大小:Pb2+>Cd2+>Ce3+.
Ce3+,Cd2+ and Pb2+ could influence the activity of amylase from porcine pancreas and competitively replace Ca2+ from amylase. The results showed that the activity of amylase was enhanced under the treatment of Ce3+,Cd2+ and Pb2+ respectively at low concerntration, but inhibited at the high concerntration. Both replacement and inhibition showed that the action was in the order: Pb2+>Cd2+>Ce3+.
洪法水,王雪峰,沈颂东,苏国兴,潘新法. Pb2+、Cd2+和Ce3+对猪胰α-淀粉酶活性的影响[J].生物化学与生物物理进展,2002,29(1):74-77
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