...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Agricultural and Food Chemistry >Size and Molecular Flexibility Affect the Binding of Ellagitannins to Bovine Serum Albumin
【24h】

Size and Molecular Flexibility Affect the Binding of Ellagitannins to Bovine Serum Albumin

机译：大小和分子柔性影响鞣花单宁与牛血清白蛋白的结合。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Binding to bovine serum albumin of monomeric (vescalagin and pedunculagin) and dimeric ellagitannins (roburin A, oenothein B, and gemin A) was investigated by isothermal titration calorimetry and fluorescence spectroscopy, which indicated two types of binding sites. Stronger and more specific sites exhibited affinity constants, K1, of 10~4—10 M~(-1) and stoichiometrics, n1, of 2—13 and dominated at low tannin concentrations. Weaker and less-specific binding sites had K2 constants of 10~3—10~5 M~(-1) and stoichiometrics, n2, of 16—30 and dominated at higher tannin concentrations. Binding to stronger sites appeared to be dependent on tannin flexibility and the presence of free galloyl groups. Positive entropies for all but gemin A indicated that hydrophobic interactions dominated during complexation. This was supported by an exponential relationship between the affinity, K1, and the modeled hydrophobic accessible surface area and by a linear relationship between Kx and the Stem—Volmer quenching constant, K_(sv).
机译：通过等温滴定热法和荧光光谱法研究了单体（维斯拉汀和pedunculagin）和二聚体鞣花单宁（roburin A，oenothein B和gemin A）与牛血清白蛋白的结合，这表明了两种结合位点。更强更具体的位点显示出亲和常数K1为10〜4-10 M〜（-1），化学计量比n1为2-13，并且在低单宁浓度下占优势。较弱和较不特异的结合位点的K2常数为10〜3-10〜5 M〜（-1），化学计量比n2为16〜30，单宁浓度较高时占主导地位。与更强位点的结合似乎取决于单宁的柔韧性和游离没食子酰基的存在。除gemin A以外的所有蛋白的正熵表明，络合过程中疏水相互作用占主导。这由亲和力K1和建模的疏水可及表面积之间的指数关系以及Kx和Stem-Volmer猝灭常数K_（sv）之间的线性关系支持。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号