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  • 标题:Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin
  • 本地全文:下载
  • 作者:Kanako MINODA ; Tatsuya ICHIKAWA ; Tomoharu KATSUMATA
  • 期刊名称:Journal of Nutritional Science and Vitaminology
  • 印刷版ISSN:0301-4800
  • 电子版ISSN:1881-7742
  • 出版年度:2010
  • 卷号:56
  • 期号:5
  • 页码:331-334
  • DOI:10.3177/jnsv.56.331
  • 出版社:Center for Academic Publications Japan
  • 摘要:The major catechins of green tea extract are (−)-epicatechin (EC), (−)-epigallocatechin (EGC), (−)-epicatechin gallate (ECg), and (−)-epigallocatechin gallate (EGCg). Recent research has indicated that catechins form complexes with human serum albumin (HSA) in blood, and differences in their binding affinity toward HSA are believed to modulate their bioavailability. In this study, we kinetically investigated the interaction between the catechins and HSA immobilized on a quartz-crystal microbalance (QCM). The association constants obtained from the frequency changes of QCM revealed interactions of ECg and EGCg with HSA that are 100 times stronger than those of EC and EGC. Furthermore, comparisons of these catechins by native-gel electrophoresis/blotting with redox-cycling staining revealed that, in a phosphate buffer, ECg and EGCg have a higher binding affinity toward HSA than EC and EGC. These observations indicate that catechins with a galloyl moiety have higher binding affinities toward HSA than catechins lacking a galloyl moiety.
  • 关键词:catechin;human serum albumin;interaction;binding affinity;galloyl moiety
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