RESUMEN
The full-length nonstructural protein P90 of rubella virus (RV) was expressed as recombinant protein in Escherichia coli bacteria, as well as in Vero cells. Monoclonal antibodies raised against the protein specifically reacted with the protein in both P90-transfected and RV infected Vero cells. Ninety human sera obtained from reconvalescents, vaccinees and patients with acute RV infection were tested for reactivity against the P90 protein. A weak immune reaction was detected only in a small minority (8%), indicating that P90 is minor immunogen for RV and is not suitable for diagnostic purposes.
Asunto(s)
Antígenos Virales/inmunología , Virus de la Rubéola/inmunología , Vacunas Sintéticas/inmunología , Proteínas no Estructurales Virales/inmunología , Animales , Anticuerpos Antivirales/sangre , Anticuerpos Antivirales/inmunología , Antígenos Virales/genética , Chlorocebus aethiops , Humanos , Ratones , Ratones Endogámicos BALB C , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/inmunología , Rubéola (Sarampión Alemán)/sangre , Virus de la Rubéola/genética , Vacunas Sintéticas/genética , Células Vero , Proteínas no Estructurales Virales/genéticaRESUMEN
Four monoclonal antibodies (MAbs) directed to native glycerophospholipid:cholesterol acyltransferase (GCAT) epitopes of Aeromonas salmonicida were isolated using an esterase capture assay. The molecular mass of this MAb-defined antigen was estimated to be 26 kDa in SDS-PAGE. Three different epitope specificities of these MAbs were demonstrated. It was shown that all 4 MAbs recognize GCAT in culture filtrates of the strain MT004 excluding the simultaneous trapping of other components. None of the MAbs react with the denatured GCAT in Western blots.
Asunto(s)
Aciltransferasas/inmunología , Aeromonas/inmunología , Anticuerpos Monoclonales/inmunología , Antígenos Bacterianos/inmunología , Aeromonas/enzimología , Animales , Anticuerpos Antibacterianos/química , Anticuerpos Antibacterianos/inmunología , Anticuerpos Monoclonales/química , Especificidad de Anticuerpos , Unión Competitiva , Electroforesis en Gel de Poliacrilamida/veterinaria , Ensayo de Inmunoadsorción Enzimática/veterinaria , Mapeo Epitopo/veterinaria , Epítopos/inmunología , Enfermedades de los Peces/inmunología , Infecciones por Bacterias Gramnegativas/inmunología , Infecciones por Bacterias Gramnegativas/veterinaria , Hibridomas , Peso Molecular , Pruebas de Precipitina/veterinaria , SalmónRESUMEN
The localization of acetylcholinesterase (AChE) as revealed either by enzyme-histochemical or by immunohistochemical methods was compared in distinct regions of the rat brain. In general, the localization of AChE observed was nearly the same, whether revealed by histochemical demonstration of its catalytic activity or by immunohistochemical detection of the enzyme molecule itself, in all regions investigated. Penetration problems of the antibodies, however, arose on strong myelin sheaths of the facial nerve, for instance, where no immunohistochemical staining was found though there was a relatively strong histochemical reaction. These problems could be partly solved by increasing the normal concentration of Triton X-100 added to the immunohistochemical solutions (0.1%) to 2.5%. Furthermore, it seems that sites containing low amounts of AChE could be better detected by the enzyme-histochemical method, whereas the depiction of structures (particularly of nerve fibres) was somewhat sharper with the immunohistochemical method.
