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CO_3^(2-)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。
The comparative studies of the denaturation of α-amlase, Ca^(2+)-free amylase and bovine serum albumin (BSA) by guanidine hydrochloride (GuHCl), guanidine carbonate (Gu_2H_2CO_3) and sodium carbonate (Na_2CO_3) were carried out by means of UV difference, fluorescence and CD spectra. The analysis of the spectra data shows that the anion CO_3^(2-) of Gu_2H_2CO_3 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 Gu_2H_2CO_3 for the denaturation of the enzyme. The possible sites of the interactions on the enzyme molecules are described.
出处
《吉林大学自然科学学报》
CSCD
1992年第4期101-105,共5页
Acta Scientiarum Naturalium Universitatis Jilinensis
