Photooxidative changes of lysozyme with 337.1 nm laser radiation.
Initial photoinduced oxidative changes in the protein lysozyme were studied using the 337.1 nm radiation from a pulsed nitrogen laser without exogenous sensitizing compounds. Irradiation of lysozyme and tryptophan in aerated solution results in the temperature and solvent dependent loss of tryptophan absorption and fluorescence, and the appearance of fluorescent "daughter products," primarily N-formyl-kynurenine and kynurenine. Exposures that resulted in 15% loss of tryptophan fluorescence produced no measurable loss in enzymatic activity. Fluorescence quenching experiments on irradiated lysozyme at low conversion percentage suggest that an exposed residue (Trp-62) is favored as an initial target of attack.
VanderMeulen
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DL
Baylor Research Foundation, Dallas, TX 75246.
Judy
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MM
D007700:Kinetics; D007834:Lasers; D009113:Muramidase / Q000378:metabolism / Q000528:radiation effects*; D010777:Photochemistry; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000528:radiation effects
D014364:Tryptophan; D009113:Muramidase