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  • (1-3)β-d-Glucan (immunolocalisation)  (1)
  • Cytochrome f  (1)
  • Golgi compartments  (1)
  • 1
    Electronic Resource
    Electronic Resource
    The zygote cell wall of Chlamydomonas reinhardii: a structural, chemical and immunological approach (1987)
    Springer
    Planta 170 (1987), S. 433-445 
    Details
    ISSN: 1432-2048
    Keywords: Cell wall ; Chlamydomonas (cell wall) ; (1-3)β-d-Glucan (immunolocalisation) ; Zygote (cell wall)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The zygote cell wall of Chlamydomonas reinhardii has been studied using structural, chemical and immunological methods. Monoclonal antibodies and polyclonal antisera that were originally raised to the major hydroxyproline-rich glycoproteins of the vegetative cell wall were used to probe the zygote wall for common antigenic components. These antibodies cross-reacted strongly and specifically with components of the zygote cell wall, and were used to show the origin, route of transport, and the location of these antigens within the zygote cell wall. The zygote cell wall contained about 10% protein, with hydroxyproline accounting for 22.5 mol % of the total amino acids present. Glucose was the most abundant sugar residue, and accounted for 56% of the total sugar present. Gas liquid chromatography-mass spectrometry showed the presence of a (1-3)β-d-glucan as the major structural polysaccharide within the zygote cell wall. The (1-3)β-d-glucan was detected and localised within the zygote cell wall by immunogold labelling of thin sections. Using an antiserum directed against (1-3)β-d-linked glucose units, this polysaccharide was found to be consistently present within the non-staining layer of both young and mature zygote cell walls. (1-3)β-d-Glucan was also detected in other wall layer using higher concentrations of antiserum. No intracellular labelling was found, indicating that the plasmamembrane is the site for the synthesis of this polysaccharide within the Chlamydomonas zygote.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402977
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  • 2
    Electronic Resource
    Electronic Resource
    Immuno-gold localization of cytochrome f, light-harvesting complex, ATP synthase and ribulose 1,5-bisphosphate carboxylase/oxygenase (1985)
    Springer
    Planta 165 (1985), S. 333-339 
    Details
    ISSN: 1432-2048
    Keywords: ATP synthase ; Cytochrome f ; Immuno-gold labelling ; Light-harvesting chlorophyll a/b protein ; Ribulose 1,5-bisphosphate carboxylase/oxygenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The proteins ribulose 1,5-bisphosphate carboxylase/oxygenase, ATP synthase, light-harvesting chlorophyll a/b protein, and cytochrome f, have been localized in mesophyll chloroplasts of barley (Hordeum vulgare L.) by electron microscopy of immunogold-labelled sections. The light-harvesting chlorophyll a/b protein and cytochrome f are shown to be present in the grana, both within the stacks and at the margins, and in the stromal membranes. Although the absolute amount of labelling for these proteins is greater in the grana than in the stromal membranes, when expressed as label/membrane length the partitioning appears approximately equal between appressed and non-appressed membranes for both the light-harvesting chlorophyll a/b protein and cytochrome f. ATP synthase is restricted to the non-appressed thylakoid membranes, and ribulose 1,5-bisphosphate carboxylase/oxygenase is uniformly distributed through the stromal contents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392229
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  • 3
    Electronic Resource
    Electronic Resource
    Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments (1987)
    Springer
    Planta 171 (1987), S. 302-312 
    Details
    ISSN: 1432-2048
    Keywords: Cell wall (glycoprotein) ; Chlamydomonas ; Glycoprotein, hydroxyproline-rich ; Golgi compartments ; O-Glycosidic linkage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A series of monoclonal antibodies and a polyclonal antiserum have been used to investigate the localisation and pathway of biosynthesis of the cell-wall hydroxyproline-rich glycoprotein 2BII in the alga Chlamydomonas reinhardii. Glyco-protein precursors were detected within the endoplasmic reticulum using a polyclonal antiserum raised to the deglycosylated 2BII. Monoclonal antibodies which are known to recognise different carbohydrate epitopes of 2BII were found to label two distinct regions of the Golgi stack. The immunolabelling results demonstrate that there is compartmentation of protein synthesis and glycosylation steps for these O-glycosidically linked glycoproteins. Newly synthesised glycoproteins are transported from the Golgi apparatus to the cell surface via two distinct routes. They then undergo assembly into a cell wall, the inner wall layer being formed first and probably functionaing as a template within which the outer crystalline wall layers are assembled.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00398675
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