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Studies on Interaction between Isorhamnetin and Bovine Serum Albumin and Effects of Several Metal Ionson Interaction by Spectrometry

ZHOU Xiuqing1, CHENG Jianhua2, SUN Lei3, XU Haoyan3, JIN Haiyan3   

  1. 1. Test Science Experiment Center, Jilin University, Changchun 130021, China; 2. College of Environment and Resources, Jilin University, Changchun 130061, China;3. College of Chemistry, Jilin University, Changchun 130012, China
  • Received:2008-04-10 Revised:1900-01-01 Online:2008-09-26 Published:2008-09-26
  • Contact: JIN Haiyan

Abstract: The interaction mechanisms of Isorhamnetin ( ISO) and bovine serum albumin (BSA), ISO and several metal ions as well as BSA and several metal ions were studied by means of ultraviolet visible absorption spectrometry and fluorescence spectroscopy. These experimental results show that the static gravitation was the major force of the combination about the interaction of ISO and bovine BSA. Flourescence of BSA was quenched by ISO with the static mechanism. The binding styles of several metal ions and ISO were studied, too. It shows the binding mechanisms of some complexes of the metal ions and ISO w ith BSA. It indicates that the interventions of metal ions affected the combination of ISO and BSA, they depressed their abilities of combination.

Key words: isorhamnetin, bovine serum albumin, fluorescence quen ching, binding constant, binding site

CLC Number: 

  • O657.3