Chicken muscle model systems were exposed to varying concentrations of lipi
d and protein fibers to clarify the role of these constituents in lipid oxi
dation. In this study, the lipid substrates examined included triacylglycer
ols, membrane phospholipid fractions, isolated phospholipid fractions, and
free fatty acids. In iron-ascorbate catalyzed systems, increases in lipid c
oncentration failed to lead to enhanced levels of oxidation at the examined
times. Lipid was therefore not considered a rate limiting factor in the ox
idation of muscle systems. Protein fibers accelerated oxidation only in sar
coplasmic reticulum (SR) membrane systems when catalyzed by iron-ascorbate.
Enhanced interaction of the low molecular weight iron with the membrane li
pids may be responsible for this unique response. Preferential oxidation of
sulfhydryl groups in protein fibers, on the other hand, could account for
the antioxidant effect displayed by protein fibers in methemoglobin catalyz
ed systems.