Glutathione peroxidase activity of human erythrocyte membranes.
Explore the source record for details and available documents.
Erythrocyte Membrane↗
Biomedical subjects
Z Földes-Papp
Publications and source records attributed to Z Földes-Papp.
Reevaluation of membrane binding of erythrocyte glutathione reductase (EC 1.6.4.2).
Data concerning membrane binding of glutathione reductase (GSSG-R) have been reexamined with respect to the following experimental conditions: 1. Haemolysis and membrane preparation; 2. influence of nonionic detergents (Triton X-100, Lubrol PX). Haemolysis and membrane preparations performed at physiological ionic strength, and reduced glutathione concentration do not give any evidence for binding of GSSG-R to the erythrocyte membrane. Under hypotonic conditions of ghost preparation about 2% of the total cellular GSSG-R activity are membrane bound, indicating weak enzyme association at low ionic strength only.
Adult↗
Suppression of exonucleolytic degradation of double-stranded DNA and inhibition of Exonuclease III by PNA.
Degradation of double-stranded DNA by Exonuclease III in the presence of complementary anti-parallel PNA was studied. It was found for the first time that the PNA suppresses the degradation of dsDNA in a sequence-specific manner as well as inhibits the activity of Exonuclease III in a non-specific way.
Base Sequence↗