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α-淀粉酶碳酸胍变性中CO32-作用的光谱学证据

Optical Evidence for CO32- Role in the Denaturation of α-Amylase by Guanidine Hydrochloride

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【作者】 张学忠吴华汪大伟程玉华

【Author】 Zhang Xuezhong, Wu Hua, Wang Dawei, Cheng Yuhua (Laboratory of Enzyme Engineering, Jilin University, Changchun)

【机构】 吉林大学酶工程实验室吉林大学酶工程实验室 长春长春长春

【摘要】 以α-淀粉酶盐酸胍变性作用为对照,利用紫外差光谱、荧光光谱和圆二色谱法研究了α-淀粉酶、脱钙α-淀粉酶和牛血清白蛋白碳酸胍及碳酸钠的变性作用。光谱数据所反映的酶分子构象变化和酶活性的变化表明,碳酸胍阴离子CO32-与酶蛋白间存在着复杂的作用,可能是碳酸胍强变性作用的重要原因之一。

【Abstract】 The comparative studies of the denaturation of α-amlase, Ca2+-free amylase and bovine serum albumin (BSA) by guanidine hydrochloride (GuHCl), guanidine carbonate (Gu2H2CO3) and sodium carbonate (Na2CO3) were carried out by means of UV difference, fluorescence and CD spectra. The analysis of the spectra data shows that the anion CO32- of Gu2H2CO3 might have some direct interaction with the molecules of α-amylase, which is one of the important factors leading to the great increase in the ability of Gu2H2CO3 for the denaturation of the enzyme. The possible sites of the interactions on the enzyme molecules are described.

【关键词】 α-淀粉酶碳酸胍变性作用
【Key words】 α-amylaseGu2H2CO3denaturation
  • 【文献出处】 吉林大学自然科学学报 ,Journal of Jilin University , 编辑部邮箱 ,1992年04期
  • 【被引频次】1
  • 【下载频次】41
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