RESUMO
Effects of allantoic fluid fractions (isolated by sedimentation and gel chromatography) on inactivation of influenza virus and lipid peroxidation in viral envelopes and phospholipid liposomes indicate the presence of both components with prooxidant effects enhancing inactivation and of endogenous antioxidants stabilizing the viral activity. The hypothesized "lipid" mechanism of inactivation (suggesting activation of lipid peroxidation in viral envelopes followed by inactivation of viral nucleoprotein) permits a satisfactory interpretation of viral material inactivation.
Assuntos
Alantoide/virologia , Vírus da Influenza A/isolamento & purificação , Alantoide/metabolismo , Animais , Antivirais , Embrião de Galinha , Vírus da Influenza A/metabolismo , Peroxidação de Lipídeos , Lipossomos , Fosfolipídeos/metabolismo , Espécies Reativas de Oxigênio , Proteínas do Envelope Viral/metabolismoRESUMO
Using the flash photolysis technique, it was found that the kinetics of recombination of carbon monoxide with ferrocytochrome P-450 LM-2 can be approximated by the sum of three exponents. Incorporation of cytochrome P-450 into liposomes prepared from microsomal lipids leads to the reduction of the number of steps to two as well as to essential changes in rate constants. Addition of type I substrates (Triton N-101, albumin) cause similar changes in the reaction kinetics. NADPH-cytochrome P-450 reductase has no effect on this process. The multistep kinetics of CO recombination with cytochrome P-450 LM-2 may be accounted for by the presence of some protein conformers. The experimental results suggest that the activity and structure of cytochrome P-450 conformers is affected by the lipid microenvironment, type I substrates and Triton N-101.