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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 630 (1980), S. 459-462 
    ISSN: 0304-4165
    Keywords: Bone resorption ; Ca^2^+ release ; Osteoclast ; Parathyroid hormone ; Platelet factor 4
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1615-6102
    Keywords: Centrin ; Chilomastix cuspidata ; Cytoskeleton ; Protist ; Tubulin ; Retortamonad
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Immunochemical techniques were used to identify and localise centrin and α-tubulin inChilomastix cuspidata, an amitochondriate “excavate flagellate”. Immunoblotting showed that the molecular mass of centrin is 20 kDa and α-tubulin is 55 kDa. Immunofluorescence microscopy localises centrin to the basal-body region of the flagellar apparatus and in a centrin-containing root which runs along the groove towards the posterior of the cell. Confocal microscopy of cells double-labelled with anticentrin and antitubulin antibodies suggests that centrin is also associated with a group of microtubules called the hook band. Centrin labelling extends for two thirds of the length of the hook band, ending in a pill-like structure. In all we distinguish five major components of the centrin root. The distribution of these proteins is discussed in terms of the functions centrin and tubulin may play in this putatively primitive protist and its relatives.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1615-6102
    Keywords: Calmodulin ; Cell plate ; Centrin ; Confocal microscopy ; Immunochemistry ; Mitosis ; Plants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Centrin and calmodulin are members of the EF-hand calcium-binding superfamily of proteins. In this study we compared localisation and immunoblotting of centrin with calmodulin in several monocot (onion and wheat) and dicot (mung bean andArabidopsis) plants. We confirmed that an anti-calmodulin antibody recognised a 17 kDa protein in all species tested and localises to the cytoplasm, mitotic matrix and with microtubules of the preprophase band and phragmoplast. In contrast, immunoblotting using anti-centrin antibodies shows that plant centrins vary from 17 to 20 kDa. Immunofluorescence microscopy with anti-centrin antibodies revealed only weak centrin immunoreactivity in the cytoplasm, nucleus, nuclear envelope, phragmoplast and mitotic matrix in meristematic cells. There was a slightly more intense perinuclear labelling in large differentiating onion cells and between separating anaphase chromosomes. While centrin is known to localise to the mitotic spindle poles in animal and algal cells, there was no appreciable immunoreactivity at the spindle poles in higher plants. In contrast, there was an intense immunofluorescence signal with anti-centrin antibodies in the developing cell plate. Further characterisation of the cell plate labelling by immunogold electron microscopy shows centrin immunoreactivity was closely associated with vesicles in the cell plate. Our observations suggest that centrin may play a role in cell plate formation.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1615-6102
    Keywords: Basal body connector ; Centrin ; Flagellar roots ; Immunoblotting ; Immunolocalisation ; Phytophthora cinnamomi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Antibodies raised against the calcium-binding protein centrin, were used to identify and localise centrin containing structures in the flagellar apparatus of zoospores and cysts of the oomycetePhytophthora cinnamomi. Immunoblotting of extracts from zoospores indicates that theP. cinnamomi centrin homologue is a 20 kDa protein. Immunofluorescence microscopy with anti-centrin antibodies reveals labelling in the flagella, the basal body connector and co-localisation along the microtubular R1 root (formerly called AR3) that runs from the right side of the basal body of the anterior flagellum into the anterior of the zoospore close to the ventral surface. The centrin (R1cen) and tubulin components of the R1 root split into four loops on the right hand side of the ventral groove and rejoin along the left hand side of the groove. The R1 root continues down the left hand side of the zoospore past the basal bodies and parallel to the R4 root. We propose that at least inP. cinnamomi there is no R2 root. Immunogold labelling confirms that centrin is a component of the basal body connector complex. When the zoospores become spherical during encystment, the R1cen pivots by approximately 90 ° with respect to the nucleus.
    Type of Medium: Electronic Resource
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