• 1 January 1984
    • journal article
    • research article
    • Vol. 44  (3) , 477-493
Abstract
NADPH-dependent microsomal lipid peroxidation (LPO) can be influenced by addition of cytoplasmic supernatant. Small quantities of [rat] hepatocellular supernatant stimulate LPO; higher concentrations are inhibitory. These opposed effects depend on the relative concentrations of Cu and Fe, either as ions or protein-bound. A mathematical model is given to predict the formation of malondialdehyde as indicator of LPO in dependence of these metals. The Cu-containing superoxide dismutase was without effect on LPO, whereas ceruloplasmin was inhibitory. Inhibition of LPO by Cu ions by TRIS buffer increased the linearity of microsomal ethylmorphine demethylase.