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首页> 外文期刊>Bulletin of the Chemical Society of Japan >Potentiometric Study on Interaction of Dodecyltrimethylammonium Bromide with alpha-Amylase
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Potentiometric Study on Interaction of Dodecyltrimethylammonium Bromide with alpha-Amylase

机译：十二烷基三甲基溴化铵与α-淀粉酶相互作用的电位研究

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摘要

The binding of dodecyltrimethylammonium bromide (DTAB) with alpha-amylase was investigated under various experimental conditions,such as pH,ionic strength,urea and protein concentration at 25degC using surfactant membrane-selective electrodes as a fast and accurate method.The obtained binding isotherms have been analyzed and interpreted using the Wyman binding potential concept.The results represent:a) the self aggregation of protein that occurs at enzyme concentrations of more than 1 mg/mL (this observation was also confirmed by light-scattering measurements),b) the binding affinity at 10~(-3) M NaBr is more than other salt concentrations,and c) in the concentration range of 3 to 5 M of urea a predominant unfolding of protein occurs.
机译：以表面活性剂膜选择电极为快速，准确的方法，在25℃下pH，离子强度，尿素和蛋白质浓度等各种实验条件下，研究了十二烷基三甲基溴化铵（DTAB）与α-淀粉酶的结合。结果表明：a）酶浓度超过1 mg / mL时发生的蛋白质自聚集（该观察结果也通过光散射测量得到证实），b）在10〜（-3）M NaBr下的结合亲和力大于其他盐浓度，并且c）在3至5 M的尿素浓度范围内，蛋白质主要发生解折叠。

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