Antioxidative effect of o-benzoquinone derivatives during CCl4-induced lipid peroxidation in the rat liver

It was found that o-benzoquinones (oBQ) inhibit the CCl4-dependent lipid peroxidation (LPO) in rat liver microsomes in vitro. The experimental data suggest that the antioxidant effect of oBQ is not due to the ability of these substances to shunt the NADPH-dependent electron transport pathways. More likely, oBQ inhibit LPO due to the ability of their reduced forms to scavenge the free radicals which induce LPO. Based on the experimental data, it was concluded that the increasing absorption of liver lipids at 230-236 nm after administration of CCl4 is due to the accumulation of reduced hydroperoxides. This process was shown to be inhibited by oBQ.     

Possible pathways of lipid peroxide reduction in the liver and their intracellular localization

Lipid peroxidase activity in rat liver was studied. Rat liver cytosolic fraction was found to be capable of reducing lipid hydroperoxides. On the contrary, no lipid hydroperoxide reduction was observed in microsomes. It was found that at least two proteins in rat liver cytosol are capable of reducing phospholipid hydroperoxides. One of them is precipitated by 33-55% at (NH4)2SO4 saturation and requires reduced glutathione (GSH) as a hydrogen donor, while the other one is precipitated by 55-80% at (NH4)2SO4 saturation and reduces phospholipid hydroperoxides in the presence of a unidentified low molecular weight cytosolic factor, but not GSH or NADPH.     

Stability of lipid oxidation products in the rat liver and pathways of their utilization

The ability of liver homogenates to utilize various lipid peroxidation products was studied. Conjugated dienes and TBA-reactive products of unsaturated fatty acid phospholipids and triglycerides were found to be more stable that the corresponding lipid hydroperoxides. It was shown that decomposition of lipid hydroperoxides in liver homogenates is due to their reduction to corresponding oxycompounds without activation of free radical reactions. The ability of lipid hydroperoxides to be reduced in liver homogenates is determined by their chemical structure and decreases in the following order: polyunsaturated fatty acids--phospholipids--triglycerides--cholesterol esters.     

Principles of selective inactivation of the virus genome. IV. The effect of UV-irradiation of phage MS2 on its binding with anti-MS2-immunoglobulins

Ultraviolet (254 nm) irradiation of the bacteriophage MS2 results in the decrease of the number of antigenic determinants exposed on the virion surface. The cross-section of the decrease, as measured by the number of anti-MS2 IgG molecules bound per virion, is 10(-16) mm2 per photon. The decrease of the phage-antibody binding proceeds after irradiation with a rate constant of about 5 x 10(-3) min-1. Since the antigenic determinants of the phage MS2 coat protein does not contain photoreactive amino acid residues, the irradiation-induced decrease of the phage antibody binding is determined, most probably, by the shielding of the antigenic determinants. Such shielding could be caused by rearrangement of coat protein molecules and/or of the capsid induced by photomodification of non-antigenic fragments of coat protein and/or of intraphage RNA.