In vitro lipid oxidation modifies proteins and functional properties of sarcoplasmic reticulum

Changes in protein and fatty acid compositions of flounder sarcoplasmic reticulum during NADH plus ascorbate-dependent lipid peroxidation in vitro were related to the ability of the sarcoplasmic reticulum to sequester Ca+2. Progressive accumulation of high-molecular-weight protein components occurred concomitantly with loss of Ca+2-sequestering activity. Part of this polymerized protein may be the dimer or trimer of Ca+2, Mg+2-ATPase. Loss in Ca+2, Mg+2-ATPase protein could account for over 60% of the polymerized protein. Rate of loss of polyunsaturated fatty acids was C22:6 greater than C20:4 greater than C20:5 greater than C22:5. Loss of polyunsaturated fatty acids and accumulation of thiobarbituric acid-reactive substances occurred concomitantly with protein polymerization.