Jelínková D, Deyl Z, Miksík I, Tagliaro F
Department of Analytical Chemistry, Institute of Chemical Technology, Prague, Czech Republic.
J Chromatogr A. 1995 Aug 11;709(1):111-9. doi: 10.1016/0021-9673(95)00164-i.
A capillary zone electrophoretic method was used to obtain profiles of solubilized rat hair keratin proteins. The same methodology was used to reveal the presence of additional protein peaks in alcohol-consuming rats. Two types of separation were investigated. Alkali-solubilized keratins from hair of rats treated for 5 weeks with 5% ethanol and 2 weeks with 10% ethanol (instead of drinking water) and from controls were analysed. Whereas under alkaline conditions (pH 9.2, 50 mM borate) an additional fraction of "low-sulphur" keratins with the highest anodic mobility of this keratin category was shown in alcohol-treated animals, acid electrophoresis carried out at pH 3.5 in phosphate buffer (50 mM) revealed the presence of two sharp peaks absent in the controls. These findings were confirmed by two-dimensional separations of carboxymethylated keratin samples. An attempt was made to identify further one of the newly occurring fractions in alcohol-consuming animals. It was revealed that the tryptic hydrolysate of "low-sulphur" proteins obtained from alcohol-consuming animals contained a peptide not found in controls.
采用毛细管区带电泳法获取溶解的大鼠毛发角蛋白的图谱。使用相同的方法来揭示饮酒大鼠中其他蛋白质峰的存在。研究了两种分离类型。分析了用5%乙醇处理5周和用10%乙醇（代替饮用水）处理2周的大鼠毛发中的碱溶性角蛋白以及对照大鼠毛发中的碱溶性角蛋白。在碱性条件下（pH 9.2，50 mM硼酸盐），经酒精处理的动物中显示出“低硫”角蛋白的另一部分，其具有该角蛋白类别中最高的阳极迁移率，而在pH 3.5的磷酸盐缓冲液（50 mM）中进行的酸性电泳显示对照中不存在的两个尖锐峰。这些发现通过羧甲基化角蛋白样品的二维分离得到证实。试图进一步鉴定饮酒动物中新出现的部分之一。结果显示，从饮酒动物获得的“低硫”蛋白质的胰蛋白酶水解产物中含有对照中未发现的一种肽。
