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Glycosylation is not needed for the intracellular transport of phytohemagglutinin in developing Phaseolus vulgaris cotyledons and for the maintenance of its biological activities

By: Contributor(s): Material type: ArticleArticleLanguage: English Description: 65(1):15-22Subject(s): LOC classification:
  • 26250
 In: Physiologia PlantarumSummary: Aprox. un 10 por ciento de la proteina total contenida en las semillas de Phaseolus vulgaris cv. Greensleeves se compone de la lectina glicoproteina, fitohemaglutinina. Se investigo si la presencia de cadenas laterales de oligosacaridos vinculados al N constituye un requisito previo para el transporte intracelular correcto de esta proteina, y si la fitohemaglutinina no glicosilada mantiene sus actividades biologicas. Se incubaron cotiledones en desarrollo cortados, en presencia de tunicamicina, para evitar la glicosilacion in vivo; se determino el destino de la proteina no glicosilada sintetizada en tales cotiledones. Se hallo que la fitohemaglutinina no glicosilada alcanza su sitio normal de acumulacion, los cuerpos proteinicos, y mantiene actividades eritroaglutinadoras y mitogenicas. (RA-CIAT)Summary: Approx. 10 percent of the total protein contained in Phaseolus vulgaris cv. Greensleeves seeds is composed of the glycoprotein lectin, phytohemagglutinin. Whether the presence of N-linked oligosaccharide side chains is a prerequisite for the correct intracellular transport of this protein and whether unglycosylated phytohemagglutinin maintains its biological activities were investigated. Excised developing cotyledons were incubated in the presence of tunicamycin to prevent glycosylation in vivo, and the fate of the unglycosylated protein synthesized in such cotyledons determined. It was found that unglycosylated phytohemagglutinin reaches its normal site of accumulation, the protein bodies, and maintains erythroagglutinating and mitogenic activities. (AS)
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Journal Article Journal Article CIAT Library Document collection CINFOS Document Collection CINFOS 26250 (Browse shelf(Opens below)) c.1 Short Loan 100042893
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Aprox. un 10 por ciento de la proteina total contenida en las semillas de Phaseolus vulgaris cv. Greensleeves se compone de la lectina glicoproteina, fitohemaglutinina. Se investigo si la presencia de cadenas laterales de oligosacaridos vinculados al N constituye un requisito previo para el transporte intracelular correcto de esta proteina, y si la fitohemaglutinina no glicosilada mantiene sus actividades biologicas. Se incubaron cotiledones en desarrollo cortados, en presencia de tunicamicina, para evitar la glicosilacion in vivo; se determino el destino de la proteina no glicosilada sintetizada en tales cotiledones. Se hallo que la fitohemaglutinina no glicosilada alcanza su sitio normal de acumulacion, los cuerpos proteinicos, y mantiene actividades eritroaglutinadoras y mitogenicas. (RA-CIAT) spa

Approx. 10 percent of the total protein contained in Phaseolus vulgaris cv. Greensleeves seeds is composed of the glycoprotein lectin, phytohemagglutinin. Whether the presence of N-linked oligosaccharide side chains is a prerequisite for the correct intracellular transport of this protein and whether unglycosylated phytohemagglutinin maintains its biological activities were investigated. Excised developing cotyledons were incubated in the presence of tunicamycin to prevent glycosylation in vivo, and the fate of the unglycosylated protein synthesized in such cotyledons determined. It was found that unglycosylated phytohemagglutinin reaches its normal site of accumulation, the protein bodies, and maintains erythroagglutinating and mitogenic activities. (AS) eng

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