ABSTRACT
Structural changes in proteins of erythrocyte membranes induced by gamma-radiation at doses of 10-10(3) Gy were studied using the method of tryptophan fluorescence quenching by acrylamide. It was found that the exposure to ionizing radiation leads to a decrease in intramolecular dynamics of membrane proteins.
Subject(s)
Erythrocyte Membrane/radiation effects , Membrane Proteins/chemistry , Erythrocyte Membrane/chemistry , Gamma Rays , Humans , Protein Conformation , Spectrometry, FluorescenceABSTRACT
The effect of the low dose gamma-irradiation (270 cGy--one-fold; 90 cGy per day during 3 days) on oxidative phosphorylation, lipid peroxidation, microviscosity of the annular and free lipids membrane, and membrane protein structural state was studied. The post-radiation influence on membrane functional activity and structural state in accordance with the irradiation regimes was established.
Subject(s)
Intracellular Membranes/metabolism , Intracellular Membranes/radiation effects , Mitochondria, Liver/metabolism , Mitochondria, Liver/radiation effects , Animals , Gamma Rays , Intracellular Membranes/ultrastructure , Lipid Peroxidation/radiation effects , Male , Membrane Fluidity/radiation effects , Membrane Proteins/metabolism , Membrane Proteins/radiation effects , Mitochondria, Liver/ultrastructure , Oxidative Phosphorylation/radiation effects , Rats , Rats, WistarABSTRACT
The influence of gamma-radiation at doses 10, 10(2) and 10(3) Gy on binding of hemoglobin to the erythrocyte membrane by inductive--resonance energy transfer in the donor-acceptor pair anthracene-hemoglobin was studied. It was found that binding of hemoglobin to the erythrocyte membrane decreases with increasing dose of gamma-radiation.
