Abstract
Binding ability of liver plasma membranes of normal rats to oxidized form of cytochrome c was more potent than that of microsomes, although this binding was dependent on the buffer concentration of the suspending solution; namely, the higher the concentration of the buffer, the less was the binding of cytochrome c to both fractions. Conversely, the bound cytochrome c was eluted more easily from microsomes than from membranes, the elution pattern also being dependent on the buffer concentration. In the liver of CCl4-administered rats, the plasma membrane binds the hemoprotein more firmly and releases it less easily than in that of normal ones. Possibility of the elevation of NADH-cytochrome c reductase activity in liver cell membranes after CCl4 administration is discussed.
