RESUMEN
Composite fluoropolymer-containing sorbents based on porous silicas were synthesized for the isolation and purification of biopolymers under nondenaturing conditions. Examples of the application of these sorbents in the separation of various mixtures of peptides and proteins and purification of nucleic acids from various sources (plasmid DNA and DNA from nucleated human blood cells) using the cartridge, column, and batch (sorption in a stirred volume) methods are presented. It was shown that the sorbents can be used in laboratory practice because they are selective to nucleic acids (DNA and RNA) and proteins. These materials combine the mechanical properties of the inorganic matrix with the specific sorption properties of the polymer phase and exhibit enhanced stability to alkaline hydrolysis. Alternative methods of preparing sorbents containing polytetrafluoroethylene, polytrifluorostyrene, and polyfluorobutadiene are described. By the example of polyfluorobutadiene-containing sorbents, a completely new method for obtaining fluorinated polymer phases was developed: the polymer phase was preliminarily formed on the surface of porous disperse carriers and was fluorinated with xenon difluoride.
Asunto(s)
Biopolímeros/aislamiento & purificación , Politetrafluoroetileno , Adsorción , ADN/aislamiento & purificación , Humanos , Politetrafluoroetileno/síntesis química , Politetrafluoroetileno/química , Proteínas/aislamiento & purificación , ARN/aislamiento & purificación , Dióxido de SilicioRESUMEN
The protein fractions precipitated by ammonium sulfate from the bovine, human and Greenland's seal blood sera enhanced the pain sensitivity of mice, rats and rabbits. The proteins fraction of the seal blood serum was divided in six subfractions by ion-exchange chromatography. One of these subfractions clearly showed hyperalgesic properties, while the others had an opposite effect. The collagenase hydrolysate of the same protein fraction had an analgetic activity. The results of this and previous studies suggest the occurrence of one more nociception-regulating protein-peptide system in mammals.
Asunto(s)
Analgésicos/farmacología , Proteínas Sanguíneas/farmacología , Animales , Proteínas Sanguíneas/aislamiento & purificación , Bovinos , Cromatografía por Intercambio Iónico , Humanos , Masculino , Ratones , Ratones Endogámicos CBA , Nalorfina/farmacología , Naloxona/farmacología , Dimensión del Dolor , Conejos , Ratas , Ratas Wistar , PhocidaeAsunto(s)
Frío/efectos adversos , Hipotermia/tratamiento farmacológico , Reno , Bazo , Extractos de Tejidos/uso terapéutico , Animales , Evaluación Preclínica de Medicamentos , Hipotermia/mortalidad , Ratones , Ratones Endogámicos C57BL , Ratones Endogámicos CBA , Extractos de Tejidos/aislamiento & purificaciónAsunto(s)
Bolsa de Fabricio/fisiología , Frío/efectos adversos , Péptidos/farmacología , Animales , Pollos , Femenino , Inmunidad Innata/efectos de los fármacos , Inyecciones Intraperitoneales , Masculino , Ratones , Ratones Endogámicos C57BL , Ratones Endogámicos CBA , Péptidos/aislamiento & purificación , SolucionesRESUMEN
The protein fraction isolated from blood of seal, Phoca groenlandica, has been found to produce hyperalgesic effect on rats exposed to thermic or electrocutaneous nociceptive stimulation, but fail to affect writhes provoked by intraperitoneal injection of acetic acid solution on mice. When combined with morphine, the fraction lowered completely its narcotic analgetic action in the above mentioned tests. On the contrary, these same proteins combined with promedol or fentanil enhanced and prolonged analgetic effect of the latter. Tested in vitro the protein showed neither opioid nor anti-opioid activity. Therefore it is reasonable to suppose that neurophysiological activity of the isolated fraction is due to the peptides formed on enzymatic hydrolysis of proteins in vivo rather than these proteins as such.
Asunto(s)
Analgésicos Opioides/farmacología , Proteínas Sanguíneas/farmacología , Dolor/fisiopatología , Phocidae/sangre , Animales , Proteínas Sanguíneas/aislamiento & purificación , Interacciones Farmacológicas , Masculino , Ratones , Ratones Endogámicos CBA , Peso Molecular , Antagonistas de Narcóticos/farmacología , Dimensión del Dolor/métodos , Ratas , Ratas Endogámicas , Receptores Opioides/efectos de los fármacos , Umbral Sensorial/efectos de los fármacosRESUMEN
We demonstrated earlier, that undecapeptide of hydra vulgaris possesses vestibulo-protective activities in cats. We also investigated potential of vestibulo-protective properties of other peptide-protein substances from hydrobiontics. The work was done on 18 cats. We used the model of L. A. Radkevich and K. B. Suri for generated vestibulo-vegetative disorders (VVD).
Asunto(s)
Caniformia , Péptidos/uso terapéutico , Phocidae , Enfermedades Vestibulares/tratamiento farmacológico , Animales , Gatos , Masculino , Péptidos/farmacología , Escopolamina/farmacología , Vestíbulo del Laberinto/efectos de los fármacosAsunto(s)
Aminoácidos/sangre , Péptidos/sangre , Animales , Bovinos , Adhesión Celular/efectos de los fármacos , División Celular/efectos de los fármacos , Línea Celular , Células Cultivadas , Cromatografía Líquida de Alta Presión , Cricetinae , Cricetulus , Focalización Isoeléctrica , Peso Molecular , Péptidos/aislamiento & purificación , Péptidos/farmacología , Espectrofotometría UltravioletaRESUMEN
This paper reports a study of the chemistry of valinomycin, enniatins and related membrane-active depsipeptides that increase alkali metal ion permeability of model and biological membranes. The antimicrobial activity of these compounds and their effect on membranes has been correlated with their cation-complexing ability. The complexing reaction has been studied by spectropolarimetric and conductimetric methods. Nuclear magnetic resonance, optical rotatory dispersion, and infrared spectrophotometric studies have revealed the coexistence of conformers of the cyclodepsipeptides in solution and have led to elucidation of the spatial structure of valinomycin, enniatin B and their K(+) complexes. The effect of the conformational properties of the cyclodepsipeptides on their complexation efficiency and selectivity, surface-active properties and behavior towards phospholipid monolayers, bimolecular phospholipid membranes and a number of biological membrane systems has been ascertained. The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies. it is suggested that the principle of conformation-dependent cation binding through iondipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.