摘要
本文通过傅里叶变换红外光谱及退卷积、曲线拟合等技术研究了碳酸钙结晶对胃蛋白酶二级结构的影响 ,结果表明 :在纯的胃蛋白酶中 ,α 螺旋、 β 折叠、转角及无规卷曲等四种结构的含量分别为2 4 38% ,2 9 91% ,39 2 2 % ,6 4 9% ;而在CaCO3 胃蛋白酶溶液中 ,四种结构的含量分别为 2 0 9% ,93 30 4 % ,4 6 0 %和 0 0 0 6 %。由此可以看出 :碳酸钙晶体的形成使胃蛋白酶的α 螺旋结构减少 ,β 折叠结构增多 ,本文讨论了这种变化的本质。
The effect of crystallization of calcium carbonate on the secondary structure of pepsin was studied by Fourier transform infrared spectroscopy, derivative, deconvolution and curve-fitting techniques in this paper. The result shows that the pure protein is compsed of 24.38 % alpha-helices, 29.91 % beta-sheets, 39.22 % beta-turns and 6.49 % random structures, and the pepsin in the CaCO3/pepsin solution is composed of 2.09% alpha-helices, 93.304% beta-sheets, 4.60% beta-tums and 0.006% random structures. From these data we can see that the alpha-helices decrease and the beta-turns increase with the formation of the crystal of calcium carbonate. The essence of these changes is discussed in the paper.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2003年第3期477-480,共4页
Spectroscopy and Spectral Analysis
基金
国家自然科学基金资助项目 (2 9971 0 0 9)