【摘要】 为了了解透析纯化过程中人发角蛋白二级结构的变化情况，用接触角测定仪、圆二色谱仪（CD）和X-射线衍射仪（XRD）等对高温氨解提取的人发角蛋白进行了分析。结果表明，透析0 h～36 h，角蛋白亲水性减小，二硫键含量增加，α-螺旋含量显著增高，无规则卷曲含量占比明显减少；透析36 h～72 h，亲水性依旧减少，二硫键含量基本不变，无规则卷曲占比显著增大。透析过程对α-螺旋和β-折叠晶区基本没有影响。更多还原

【Abstract】 In order to understand the changes of the secondary structure of human hair keratin during dialysis and purification, the human hair keratin extracted by high temperature ammonolysis was analyzed by contact angle analyzer, circular dichroism(CD) and X-ray diffraction(XRD). The results showed that during 0 h-36 h of dialysis, the hydrophilicity of keratin decreased, and the content of disulfide bond increased. The α-helix content increased significantly, and the proportion of random curl content decreased significantly. During 36 h-72 h of dialysis, the hydrophilicity still decreased, the disulfide bond content remained basically unchanged, and the proportion of irregular curl increased significantly. The dialysis process had little effect on α-helix and β-folded crystal region.更多还原