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  • Articles: DFG German National Licenses  (3)
  • Immunocytochemistry  (2)
  • 34.50.H  (1)
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  • Articles: DFG German National Licenses  (3)
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Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture (1995)
    Springer
    Cell & tissue research 280 (1995), S. 415-425 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Epididymis ; Efferent ducts ; Cell culture ; Immunocytochemistry ; Immunoprecipitation ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid α-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, β-hexosaminidase (N-acetylglucosaminidase) and α-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; β-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and β-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307815
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture (1995)
    Springer
    Cell & tissue research 280 (1995), S. 415-425 
    Details
    ISSN: 1432-0878
    Keywords: Epididymis ; Efferent ducts ; Cell culture ; Immunocytochemistry ; Immunoprecipitation ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid α-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, β-hexosaminidase (N-acetylglucosaminidase) and α-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; β-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and β-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307815
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Impact parameter dependence ofL-shell vacancy production in slow Kr-Kr and Xe-Xe collisions (1987)
    Springer
    The European physical journal 6 (1987), S. 131-144 
    Details
    ISSN: 1434-6079
    Keywords: 34.50.H
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The impact parameter dependence ofL-shell vacancy production in slow Kr-Kr and Xe-Xe collisions has been investigated both experimentally and theoretically. For collision energies between 711 keV and 2.49 MeV collisionally inducedL x-rays have been observed in coincidence with scattered ions. The experimental data are compared with theoretical predictions deduced from seven-state adiabatic 1 φ u −1 δ u −4 π u −3 π u −2 π u -4 σ u −3 σ u coupled-channel calculations. Contrary to similar calculations performed previously, no approximations regarding the dependence of molecular-orbital energies and coupling matrix elements on internuclear separation have been introduced in the present calculations. For large impact parameters, agreement between experiment and theory is found on an absolute scale. For smaller impact parameters, the experimental data tend to be consistently larger than the theoretical predictions. The relative deviations for Kr-Kr collisions with impact energy smaller than 2 MeV and for Xe-Xe collisions can be parametrised by means of universal functions depending only on the minimum internuclear distanceR 0 reached in the collision. This finding is discussed in terms of possible contributions from direct molecular-orbital ionisation and of anR 0-dependence of the heavy-ion induced fluorescence yield.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01384600
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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