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  • 1
    Electronic Resource
    Electronic Resource
    Phenylalanine ammonia-lyase and chalcone synthase in glands ofPrimula kewensis (W. Wats): immunofluorescence and immunogold localization (1995)
    Springer
    Planta 196 (1995), S. 712-719 
    Details
    ISSN: 1432-2048
    Keywords: Chalcone synthase ; Farina ; Flavonoid biosynthesis ; Gland ; Phenylalanine ammonia-lyase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS) were localized by indirect immunofluorescence and immunogold labeling in glands ofPrimula kewensis. Both enzymes were exclusively present in the head cells of the glands. Phenylalanine ammonialyase was located in the regions of the dense tubular endoplasmic reticulum and occasionally found in more or less spherical organelles that have not yet been identified. Furthermore, an appreciable proportion of the enzyme protein was associated with the plasmalemma and the cell wall of the head cell. In contrast, the occurrence of CHS was restricted to the spherical, unidentified cell compartments. Our findings indicate that the gland cells have the potential for flavonoid biosynthesis. When a mutant ofP. kewensis forming structurally intact glands but incapable of farina excretion was studied, neither PAL nor CHS were found in the head cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01106765
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Phenylalanine ammonia-lyase and chalcone synthase in glands of Primula kewensis (W. Wats): immunofluorescence and immunogold localization (1995)
    Springer
    Planta 196 (1995), S. 712-719 
    Details
    ISSN: 1432-2048
    Keywords: Chalcone synthase ; Farina ; Flavonoid biosynthesis ; Gland ; Phenylalanine ammonia-lyase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS) were localized by indirect immunofluorescence and immunogold labeling in glands of Primula kewensis. Both enzymes were exclusively present in the head cells of the glands. Phenylalanine ammonialyase was located in the regions of the dense tubular endoplasmic reticulum and occasionally found in more or less spherical organelles that have not yet been identified. Furthermore, an appreciable proportion of the enzyme protein was associated with the plasmalemma and the cell wall of the head cell. In contrast, the occurrence of CHS was restricted to the spherical, unidentified cell compartments. Our findings indicate that the gland cells have the potential for flavonoid biosynthesis. When a mutant of P. kewensis forming structurally intact glands but incapable of farina excretion was studied, neither PAL nor CHS were found in the head cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197336
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    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
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