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  • 1
    Electronic Resource
    Electronic Resource
    Organization of centromeres in the decondensed nuclei of mature human sperm (1993)
    Springer
    Chromosoma 102 (1993), S. 509-518 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The localization of centromeres in mature human sperm was shown by immunofluorescent labeling and nonisotopic in situ hybridization. In the decondensed nucleus structural elements (dimers, tetramers, linear arrays and V shape structures) formed by individual centromeres of nonhomologous chromosomes were observed. They organize the compact chromocenter, which was shown for nuclei decondensed to a low extent. The chromocenter is buried inside the nucleus; in contrast, telomeric regions of chromosomes were tentatively localized on the periphery. Thus, a gross architecture, which can influence selective unpackaging of the paternal genome upon fertilization, exists in human sperm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00368344
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of a rhodopsin-like protein in the lipochondria in photosensitive neurons of Aplysia californica (1986)
    Springer
    Cell & tissue research 244 (1986), S. 115-120 
    Details
    ISSN: 1432-0878
    Keywords: Neurons ; Lipochondria ; Rhodopsin ; Immunocytochemistry ; Aplysia californica
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Polyclonal antibodies directed against squid opsin were used in immunocytochemical and immunoblot experiments to identify a rhodopsin-like protein in photosensitive neurons of Aplysia. Aldehyde-fixed abdominal and cerebral ganglia were embedded in paraffin for peroxidase anti-peroxidase analysis or used whole for immunofluorescence studies. Ganglia were embedded in Lowicryl K4M for electron-microscope immunocytochemistry. In both the cerebral and abdominal ganglia, light-microscope immunocytochemical results showed reaction product deposited around the neuronal cell periphery corresponding in position to the lipochondria. In the abdominal ganglion, the giant cell R2, located in the right rostral quarter, and neurons in the right caudal quarter were consistently labeled with anti-opsin. Electron-microscopic studies demonstrated ferritin-labeling of the lipochondria in R2 and other immunoreactive neurons. Immunoblot analysis of R2 and cerebral neuron extracts was used to identify two prominent immunoreactive protein bands at 85000 and 67500 molecular weight.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218388
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  • 3
    Electronic Resource
    Electronic Resource
    The abundant 19-kilodalton protein associated with human sperm nuclei that is related to seminal plasma α-inhibins (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 36 (1993), S. 164-173 
    Details
    ISSN: 1040-452X
    Keywords: Basic proteins ; Semenogelin processing ; Sperm head ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A basic protein with a relative molecular mass of 19 kDa has been identified and isolated to purity from sonication-resistant, partially demembranized human sperm nuclei. Several criteria prove that this is the unique sperm-specific protein, which was previously thought to be a sperm/testis histone. Partial primary structure sequencing demonstrates homologies with human seminal α-inhibins and semenogelin. From the sequence and Western-blotting data with antibodies against basic seminal inhibin-like peptide, we propose that this 19-kD protein is a product of 52-kDa semenogelin processing. The 19-kDa protein was not found among seminal plasma proteins and may be protected from further cleavage into inhibin-like peptides by its association with the sperm head Immunofluorescence data indicate its localization in the nuclear periphery, with preferential concentration at the acrosome calyx boundary. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080360207
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    Paper (German National Licenses)
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