RESUMEN
The structure of LB films of protein-polyelectrolyte complexes transferred onto the pyrographite surface was studied by STM. The images of the films obtained at various protein concentrations in the water subphase and different values of surface pressure were captured. The topology of the surface covered by one or three layers of the films studied was investigated. It is shown that at a protein concentration of 1 mg/ml in the water subphase, the films are composed of aggregated protein molecules, and their structure has an insular character. An increase in the number of transferred layers up to three results in a virtually complete covering of the surface. A decrease in the protein concentration in the water subphase to 1 microgram/ml enabled us to prepare films consisting of individual non-aggregated protein molecules.
Asunto(s)
Anticuerpos/análisis , Enzimas/análisis , Proteínas de la Membrana/ultraestructura , Microscopía de Túnel de Rastreo , Electrólitos/química , Glucosa Oxidasa/análisis , Proteínas de la Membrana/química , Monoaminooxidasa/análisisRESUMEN
A technique for forming Langmuir films from antibodies based on an amphiphilic polyelectrolyte was developed. The physicochemical and immunochemical properties of the Langmuir films obtained were studied. The interaction of HBsAg with the films was found to be described by a model with one binding site, whereas that of HBsAg with antibodies adsorbed on a polystyrene plate, by a model with a positive cooperativity. The use of the novel Langmuir films from antibodies increases the sensitivity of the immunoenzyme assay.
Asunto(s)
Electrólitos/química , Fragmentos Fab de Inmunoglobulinas/química , Membranas Artificiales , Polímeros/química , Tensoactivos/química , Animales , Electrólitos/metabolismo , Cabras , Antígenos de Superficie de la Hepatitis B/química , Antígenos de Superficie de la Hepatitis B/inmunología , Concentración de Iones de Hidrógeno , Fragmentos Fab de Inmunoglobulinas/metabolismo , Metilmetacrilato , Metilmetacrilatos/química , Concentración Osmolar , Polímeros/metabolismo , Propiedades de Superficie , Tensoactivos/metabolismo , TermodinámicaRESUMEN
The activity of a neurospecific enzyme of tyrosine hydroxylase (TH) in monomolecular films formed onto solid surface was studied. The data obtained show that the formation of two-dimensional films onto negative-charge surfaces by the Langmuir-Schafer technology does not lead to the inactivation of the enzyme. Neuroleptic trifluoperazine increased the activity of TH. Monomolecular films of TH may be used as a sensitive element of biosensors for primary monitoring of neuroleptic-like compounds.