Abstract
Ozone is shown to react with lysozyme in reverse micelles formed by 0.1 M sodium di-2-ethylhexylsulfosuccinate and 1.2-3 M water (pH 7.4) in isooctane solvent. The reaction of ozone is assessed by the oxidation of tryptophan residues in the protein to N-formylkynurenine. Cosolubilization of oleate in lysozyme-containing reverse micellar solutions at concentrations of 0.5-10 mM results in a progressive inhibition (19% to 82%) of the oxidation of tryptophan residues with a concentration for 50% inhibition around 2 mM. At this concentration of oleate, the magnitude of inhibition is independent of the micelle size and concentration, the overall interfacial area of reverse micelles, and the amount of ozone employed. These findings are discussed in terms of competitive reactions of ozone with unsaturated fatty acids and proteins in the lung lining fluid and in biological membranes.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
