RESUMEN
Interaction of phosphatidyl choline liposomes with erythrocytes during spontaneous lysis of the latter has been studied. It is shown that hemoglobin which is released during the lysis of erythrocytes is found by liposomes which in their turn are absorbed on the external erythrocyte surface. In this case the binding of hemoglobin by liposomes takes place with a greater speed than its release during erythrocyte lysis and is accompanied by a change in its conformation. Possibilities of the microcalorimetry methods for studying the interaction of liposomes with erythrocytes under the conditions mentioned above are considered.
Asunto(s)
Eritrocitos/metabolismo , Hemólisis/fisiología , Liposomas/metabolismo , Fosfatidilcolinas/metabolismo , Animales , Perros , Hemoglobinas/metabolismo , Hemólisis/efectos de los fármacos , Unión Proteica , Conformación Proteica/efectos de los fármacosRESUMEN
Physico-chemical parameters of membranes of skeletal muscles' sarcoplasmic reticulum in antioxidant insufficiency, which was modelled by excluding alpha-tocopherol from the animals ration, and after treatment with phenol antioxidant ionol were studied. It was shown that activation of lipid peroxidation in vitamin E insufficiency results in a significant lowering of microviscosity of lipid bilayer membranes of sarcoplasmic reticulum. Using polarography significant changes in membrane protein conformation were revealed, which were characterized by lowering of integrity and by disorganization of protein globules. Treatment of animals with antioxidant insufficiency with ionol led to certain normalization of changes of physico-chemical characteristics of the learned membrane structures caused by lipid peroxidation.
Asunto(s)
Antioxidantes , Músculos/efectos de los fármacos , Peróxidos/farmacología , Retículo Sarcoplasmático/efectos de los fármacos , Animales , Hidroxitolueno Butilado/farmacología , Membrana Celular/química , Membrana Celular/efectos de los fármacos , Femenino , Membrana Dobles de Lípidos , Peroxidación de Lípido , Músculos/metabolismo , Polarografía , Ratas , Ratas Endogámicas , Retículo Sarcoplasmático/metabolismo , Espectrofotometría UltravioletaRESUMEN
The fluorescence and polarography methods are used to establish certain differences in conformation characteristics of transcriptionally active and repressed forms of rat liver chromatin. The data obtained prove the nucleo-soma ability to aggregation in the repressed chromatin and confirm a decondensed character of packing in transcriptionally active chromatin. It is supposed that these peculiarities are connected with different content of calcium and iron ions in the studied fractions of chromatin. Lipids, being the components of chromatin fractions, are packed with proteins in a form of bilayer structure. The packing character is similar in the both chromatin fractions. But microviscosity of the lipid bilayer in transcriptionally active chromatin is significantly lower than that in the repressed one and this may be one of reasons of different transcriptional activity and ability to peroxidation of the studied chromatin forms.