The Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Algae

The intrinsic steady-state fluorescence due to tryptophan has been obtained from monospecific cultures of fourteen plankton algae of various genera. Fluorescence decay profiles of protein tryptophan residues were obtained for eight marine plankton algae. Each organism exhibits a strong maximum in its emission spectrum at 320–340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 320–340 nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein tryptophan fluorescence has been described. 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 algae. Direct application will likely be found in combination with the measurement of other luminescence parameters.

[1]  in chief George M. Garrity Bergey’s Manual® of Systematic Bacteriology , 1989, Springer New York.

[2]  D. Britt,et al.  An Ultraviolet (242 nm Excitation) Resonance Raman Study of Live Bacteria and Bacterial Components , 1987 .

[3]  W. H. Nelson,et al.  The Steady-State and Decay Characteristics of Primary Fluorescence from Live Bacteria , 1987 .

[4]  W. Nelson,et al.  The Resonance Raman Microprobe Detection of Single Bacterial Cells from a Chromobacterial Mixture , 1987 .

[5]  W. Nelson,et al.  A Resonance Raman Microprobe Study of Chromobacteria in Water , 1986 .

[6]  W. Nelson,et al.  Steady-State and Decay Characteristics of Protein Tryptophan Fluorescence from Bacteria , 1986 .

[7]  W. Nelson,et al.  The Rapid Identification of Bacteria Using Time-Resolved Fluorescence and Fluorescence Excitation Spectral Methods , 1985 .

[8]  I. Warner,et al.  Spectral «fingerprinting» of phytoplankton populations by two-dimensional fluorescence and Fourier-transform-based pattern recognition , 1985 .

[9]  A. Szabo,et al.  Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study. , 1983, Biophysical journal.

[10]  J. Knutson,et al.  Decay-associated fluorescence spectra and the heterogeneous emission of alcohol dehydrogenase. , 1982, Biochemistry.

[11]  L. Brand,et al.  Time-resolved fluorescence and anisotropy decay of the tryptophan in adrenocorticotropin-(1-24). , 1981, Biochemistry.

[12]  C. J. Schmidt,et al.  Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. , 1981, Biochemistry.

[13]  S. Cockle,et al.  TIME‐RESOLVED FLUORESCENCE SPECTRA OF TRYPTOPHAN IN MONOMERIC GLUCAGON * , 1981, Photochemistry and photobiology.

[14]  R. J. Robbins,et al.  Time-resolved fluorescence from biological systems: tryptophan and simple peptides , 1980, Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences.

[15]  I. Warner,et al.  Multiparameter appraoch to the "fingerprinting" of fluorescent Pseudomonads. , 1980, Clinical chemistry.

[16]  I. Warner,et al.  Identification of fluorescent Pseudomonas species. , 1980, Clinical chemistry.

[17]  A. Szabo,et al.  The time resolved emission spectra of peptide conformers measured by pulsed laser excitation. , 1980, Biochemical and biophysical research communications.

[18]  W. H. Nelson,et al.  A Resonance Raman Method for the Rapid Detection and Identification of Bacteria in Water , 1980 .

[19]  J. Brochon,et al.  Time resolved spectroscopy of the tryptophyl fluorescence of the E. coli LAC repressor. , 1977, Biochemical and biophysical research communications.

[20]  A. Grinvald,et al.  The fluorescence decay of tryptophan residues in native and denatured proteins. , 1976, Biochimica et biophysica acta.

[21]  L. Andrews,et al.  FLUORESCENCE CHARACTERISTICS OF INDOLES IN NON‐POLAR SOLVENTS: LIFETIMES, QUANTUM YIELDS AND POLARIZATION SPECTRA , 1974 .

[22]  C. Conti,et al.  Non-exponential decay of indole fluorescence--the red-edge effect. , 1974, Biochemical and biophysical research communications.

[23]  J. Lakowicz,et al.  Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. , 1973, Biochemistry.

[24]  M. Kronman,et al.  THE FLUORESCENCE OF NATIVE, DENATURED AND REDUCED‐DENATURED PROTEINS * , 1971 .

[25]  P. Cook Contributed Papers. Joint meeting with the Phycological Section, Botanical Society of America. , 1970 .

[26]  S. Lehrer The selective quenching of tryptophan fluorescence in proteins by iodide ion: lysozyme in the presence and absence of substrate. , 1967, Biochemical and biophysical research communications.

[27]  M. Droop A procedure for routine purification of algal cultures with antibiotics , 1967 .

[28]  Sergei V. Konev,et al.  Fluorescence and Phosphorescence of Proteins and Nucleic Acids , 1967, Springer US.

[29]  H. A. Neufeld,et al.  CHEMILUMINESCENCE OF LUMINOL IN THE PRESENCE OF HEMATIN COMPOUNDS. , 1965, Analytical biochemistry.

[30]  R. G. Crounse,et al.  Fluorescence Assay in Biology and Medicine , 1963 .

[31]  R. Guillard,et al.  Studies of marine planktonic diatoms. I. Cyclotella nana Hustedt, and Detonula confervacea (cleve) Gran. , 1962, Canadian journal of microbiology.

[32]  F. Teale,et al.  The ultraviolet fluorescence of proteins in neutral solution. , 1960, The Biochemical journal.

[33]  G. Weber,et al.  Ultraviolet fluorescence of the aromatic amino acids. , 1957, The Biochemical journal.

[34]  S. Moore,et al.  Chromatography of amino acids on starch columns; solvent mixtures for the fractionation of protein hydrolysates. , 1949, The Journal of biological chemistry.

[35]  S. P. Parker Synopsis and classification of living organisms , 1982 .

[36]  W. J. Irwin,et al.  Analytical pyrolysis : a comprehensive guide , 1982 .

[37]  A. Szabo,et al.  Fluorescence decay of tryptophan conformers in aqueous solution , 1980 .

[38]  I Munro,et al.  Subnanosecond motions of tryptophan residues in proteins. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[39]  J. Winefordner Practical fluorescence: theory, methods, and techniques , 1974 .

[40]  V. Frattali,et al.  NATIVE AND UNFOLDED STATES OF PEPSINOGEN. II. THE KINETICS OF THE STRUCTURAL TRANSITION INDUCED BY UREA. , 1965, The Journal of biological chemistry.

[41]  R. Sager,et al.  Chloroplast structure in green and yellow strains of Chlamydomonas. , 1954, Experimental cell research.