STEADY-STATE AND DECAY CHARACTERISTICS OF PROTEIN TRYPTOPHAN FLUORESCENCE FROM BACTERIA.

Authors

R. A. Dalterio, University of Rhode Island
W. H. Nelson, University of Rhode Island
D. Britt, University of Rhode Island
J. Sperry, University of Rhode Island
D. Psaras, University of Rhode Island
J. F. Tanguay, University of Rhode Island
S. L. Suib, University of Rhode Island

Document Type

Article

Date of Original Version

1-1-1986

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.

Publication Title, e.g., Journal

Applied Spectroscopy

Volume

40

Issue

1

Citation/Publisher Attribution

Dalterio, R. A., 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.." Applied Spectroscopy 40, 1 (1986). doi: 10.1366/0003702864815439.