Spectral Response of Hemoproteins to the Effects of Peroxidized Phosphatidylcholine and Its Derivatives
摘要
The effect of UV-irradiated phosphatidylcholine (or oleic acid) on a number of heme-containing proteins (human hemoglobin, equine myoglobin, horseradish peroxidase, and bovine cytochrome C) manifested as the development of a differential spectrum in the Soret band (ΔD) during their interaction that was found to be characteristic for hemoproteins of both animal and plant origin based on an analysis of spectral changes in the 403–423 nm wavelength range. It was shown that the intensity of the spectral response under the specified conditions was distributed in the following order: peroxidase ≥ myoglobin ≥ hemoglobin ≥ cytochrome C. The determination of peroxidase as the best indicator for the detection of peroxidized lipids by a spectroscopic method can be used while conducting clinical and biochemical studies involving it and for developing new methods of diagnosing the body's ability to protect against oxidative stress and predicting its ability to recover from diseases of varying severity.