期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 75, 期 3, 页码 1024-1029出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2009.12.044
关键词
Prulifloxacin; Pepsin; Fluorescence quenching; Stern-Volmer equation; The Forster's resonance energy transfer theory
类别
The interaction between prulifloxacin, a kind of new oral taking antibiotic and pepsin, a kind of enzyme in the stomach has been investigated in vitro under a simulated physiological condition by different spectroscopic methods. The intrinsic fluorescence of pepsin was strongly quenched by prulifloxacin. This effect was rationalized in terms of a static quenching procedure. The binding parameters have been evaluated by fluorescence quenching methods. The negative value of AGO reveals that the binding process is a spontaneous process. The binding distance R between donor (pepsin) and acceptor (prulifloxacin) was obtained according to the Forster's resonance energy transfer theory and found to be 0.95 nm. The results obtained herein will be of biological significance in pharmacology and clinical medicine. Crown Copyright (C) 2010 Published by Elsevier B.V. All rights reserved.
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