期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 75, 期 5, 页码 1506-1510出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2010.02.007
关键词
Hyperoside; Bovine serum albumin; Fluorescence quenching; Tachiya model
类别
资金
- Scientific Research Common Program of Beijing Municipal Commission of Education [KM200810025025]
- Funding Project for Academic Human Resources Development in Institutions of Higher Learning Under the Jurisdiction of Beijing Municipality [PHR201007114]
The interaction between hyperoside and bovine serum albumin (BSA) was examined by fluorescence spectroscopy at 298, 304, and 310 K. The spectroscopic data were analyzed using Tachiya model and Stern-Volmer equation to determine the binding sites and apparent binding constant between hyperoside and BSA. For Tachiya model, both binding sites and apparent binding constants increased with the increasing of temperature, whereas for Stern-Volmer equation, the corresponding binding constants. decreased as temperature increasing and the binding sites were independent of temperature. The positive sign of enthalpy change (Delta H) and entropy change (Delta S) suggested that hydrophobic forces played a major role in the interaction. Synchronous fluorescence spectra indicated that the conformation of protein was perturbed by the interaction of hyperoside with BSA. Moreover, the presence of metal ion affected the hyperoside-BSA binding. (C) 2010 Elsevier B.V. All rights reserved.
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