These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Study on the interaction between salicylic acid and catalase by spectroscopic methods.
    Author: Wu Y.
    Journal: J Pharm Biomed Anal; 2007 Jul 27; 44(3):796-801. PubMed ID: 17459641.
    Abstract:
    The interaction between catalase (CAT) and salicylic acid (SA) was studied by fluorescence and UV-vis spectroscopic techniques. The quenching mechanism of fluorescence of BSA by CAT was discussed to be a static quenching procedure. The number of binding sites n and apparent binding constant K was measured by fluorescence quenching method. The thermodynamics parameter DeltaH, DeltaG, DeltaS were calculated. The results indicate the binding reaction was both entropy-driven and the enthalpy-driven, and the hydrogen bond and van der Waals force played major role in the binding reaction. The binding sites of SA with CAT was investigated to be approached the microenvironment of Trp by the synchronous fluorescence spectrometry. The distance r between donor (CAT) and acceptor (SA) was obtained according to Förster theory of non-radioactive energy transfer.
    [Abstract] [Full Text] [Related] [New Search]