Paper
2 May 2003 Spectral analysis of light emitted during the oxidation of lipids and proteins
Julio F. Turrens, Eric Robinson, Scott Freeman, Benedict F. George III
Author Affiliations +
Abstract
Oxidative stress is associated with a variety of pathological processes of clinical relevance. Some of the intermediates generated during the chain reactions associated with oxidation of lipids and proteins are electronically excited and decay emitting photons, which may be detected with the help of sensitive photomultipliers. This technique has been used to monitor oxidative stress in a variety of scenarios including intact organs in vivo or in vitro, and simple models such as proteins and lipids exposed to oxidants. The main drawback of this technique is that the emission of light is extremely weak and it is subjected to substantial interference from spurious sources. In addition, the quantum efficiency of photomultipliers varies with wavelength making it even more difficult to collect reliable data using photomultipliers sensitive to relatively broad spectral ranges. In order to identify the peak emission wavelengths in the visible region, we exposed model systems (proteins, lipids and amino acids) to peroxynitrite and sources of hydroxyl and alcoxyl radicals, analyzing the emission of light with interference filters. The results indicate that the peak emission for most biological models occurs between 450 and 700 nm. The emission at higher wavelengths (lower energy levels) was observed mostly in the presence of less powerful oxidants such as tert-butyl hydroperoxide.
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Julio F. Turrens, Eric Robinson, Scott Freeman, and Benedict F. George III "Spectral analysis of light emitted during the oxidation of lipids and proteins", Proc. SPIE 5031, Medical Imaging 2003: Physiology and Function: Methods, Systems, and Applications, (2 May 2003); https://doi.org/10.1117/12.480409
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KEYWORDS
Systems modeling

Photomultipliers

Proteins

Quantum efficiency

Chemiluminescence

Oxidation

Hydrogen

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