Asunto(s)
Escherichia coli/metabolismo , Genes Sintéticos , Interferón-alfa/genética , Biosíntesis de Péptidos , Secuencia de Aminoácidos , Aminoácidos/análisis , Secuencia de Bases , Cromatografía Líquida de Alta Presión , Expresión Génica , Humanos , Hidrólisis , Datos de Secuencia Molecular , Péptidos/metabolismo , Plásmidos , Homología de Secuencia de Ácido NucleicoRESUMEN
Constituent proteins of human influenza virus A have been separated by reverse-phase HPLC on Polysil ODS-500. Their homogeneity is confirmed by the data of amino acid composition, Edman analysis and gel electrophoresis.
Asunto(s)
Virus de la Influenza A/metabolismo , Proteínas Virales/aislamiento & purificación , Secuencia de Aminoácidos , Cromatografía Líquida de Alta Presión , Electroforesis en Gel de Poliacrilamida , Datos de Secuencia Molecular , Albúmina Sérica Bovina/aislamiento & purificación , Proteínas Virales/genéticaRESUMEN
The receptor properties of influenza virus A/Kiev/59/79 R (H1N1) and a number of its polypeptide fragments containing the aminoacids (from the 1st to 272d) of the heavy chain were studied. Two kinds of radioimmunoassay were used to test hemagglutinin or its polypeptide fragment interactions with cellular receptors. The studied polypeptides and hemagglutinin are shown to be capable of specific interactions with the receptors on the cell surface. The main linear fragment of hemagglutinin recognizing cellular receptors is localized within a polypeptide fragment including 1st-272d aminoacids of the heavy chain of hemagglutinin. The breaks of all the the S-S linkages including the ones linearly and spatially close to the receptor "pocket" of the bridge 95-135 do not affect significantly the receptor properties of the polypeptide.