Stabilization of solutions of feather keratins by sodium dodecyl sulfate
Stabilization of solutions of feather keratins by sodium dodecyl sulfate
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DOI：
10.1006/jcis.2001.7673
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发表时间：
2001-08-01
影响因子：
9.9
通讯作者：
Feijen, J
中科院分区：
文献类型：
--
作者：
Schrooyen, PMM;Dijkstra, PJ;Feijen, J
采用尿素和巯基乙醇水溶液从鸡毛中提取羽毛角蛋白。过滤不溶性残余物后，获得羽毛角蛋白溶液。通过透析去除2-巯基乙醇和尿素导致角蛋白多肽链的聚集和半胱氨酸残基的氧化，以提供凝胶。在透析前向角蛋白溶液中加入十二烷基硫酸钠（SDS）可防止角蛋白链的广泛聚集。研究了加入不同量的SDS对透析过程中多肽链聚集速率和半胱氨酸残基氧化速率的影响。用尺寸排阻色谱法，发现较低的初始SDS/角蛋白比率（0.125- 0.5g SDS/g角蛋白）导致较大的SDS-角蛋白复合物。这表明形成了更多的分子间交联。较高的SDS-角蛋白比率（l-2g SDS/g角蛋白）导致小的SDS-角蛋白复合物，其大小与角蛋白单体相当。高含量的SDS似乎阻止了不同角蛋白链之间的氧化反应，导致更多的分子内二硫键形成。(C)北京：科学出版社.
Feather keratins were extracted from chicken feathers with aqueous solutions of urea and 2-mercaptoethanol. After filtration of the insoluble residue, a feather keratin solution was obtained. Removal of 2-mercaptoethanol and urea by dialysis resulted in aggregation of the keratin polypeptide chains and oxidation of the cysteine residues to afford a gel. The addition of sodium dodecyl sulfate (SDS) to the keratin solution prior to dialysis prevented extensive aggregation of the keratin chains. The effect of the addition of various quantities of SDS on the rate of aggregation of the polypeptide chains and the rate of oxidation of cysteine residues during dialysis was studied. With size exclusion chromatography, it was found that lower initial SDS/keratin ratios (0.125-0.5 g SDS/g keratin) resulted in larger SDS-keratin complexes. This indicates that more intermolecular cross-links had formed. Higher SDS-keratin ratios (1-2 g SDS/g keratin) resulted in small SDS-keratin complexes, comparable in size to the keratin monomer. High amounts of SDS seemed to prevent the oxidation reaction between different keratin chains, resulting in more intramolecular disulfide bond formation. (C) 2001 Academic Press.