OSA's Digital Library

Applied Spectroscopy

Applied Spectroscopy

| PUBLISHED BY SAS — AVAILABLE FROM SAS AND OSA

  • Vol. 40, Iss. 1 — Jan. 1, 1986
  • pp: 86–90

Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Bacteria

R. A. Dalterio, W. H. Nelson, D. Britt, J. Sperry, D. Psaras, J. F. Tanguay, and S. L. Suib

Applied Spectroscopy, Vol. 40, Issue 1, pp. 86-90 (1986)


View Full Text Article

Acrobat PDF (589 KB)





Browse Journals / Lookup Meetings

Browse by Journal and Year


   


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

Share
Citations
  • Export Citation/Save Click for help

Abstract

The intrinsic steady-state fluorescence and fluorescence decay of Staphylococcus epidermidis, Pseudomonas fluorescens, Enterobacter cloacae, Escherichia coli, and Bacillus subtilis have been observed. Each organism exhibits a strong maximum in its emission spectrum at 330-340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 330-340-nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein-tryptophan fluorescence has been described by two exponential functions in all cases. The observation that characteristic protein-tryptophan fluorescence lifetimes have been obtained for each organism suggests that measurements of fluorescence lifetimes may be helpful in the rapid characterization of bacteria. Direct application will most likely be found in combination with the measurement of other luminescence parameters.

Citation
R. A. Dalterio, W. H. Nelson, D. Britt, J. Sperry, D. Psaras, J. F. Tanguay, and S. L. Suib, "Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Bacteria," Appl. Spectrosc. 40, 86-90 (1986)
http://www.opticsinfobase.org/as/abstract.cfm?URI=as-40-1-86


Sort:  Journal  |  Reset

References

References are not available for this paper.

Cited By

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited