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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 87 (1987), S. 13-19 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of the purple tartrate-resistant, iron-containing acid phosphatase in the bovine spleen was studied by enzyme histochemistry at the light and electron microscopic levels as well as by immunohistochemistry. The purple phosphatase was localized only in lysosome-like organelles of cells belonging to the reticulo-phagocytic system. The same cells were identified as containing large iron(III)-deposits as ferritin in homogeneously granular accumulations and freely in the cytoplasm, or as hemosiderin in siderosomes. The phagocytosing cells containing purple phosphatase and ferritin often had close contact with clusters of aged and deformed erythrocytes. A possible catabolic role of the purple enzyme as a phosphatase degrading phosphoproteins of the erythrocyte membrane and the cytoskeleton was assumed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A tartrate-resistant purple acid phosphatase was localized in human and bovine alveolar macrophages by enzyme- and immuno-histochemistry using an antibody to bovine spleen purple phosphatase. The enzyme could be detected in human and bovine lung tissues as well as on cytospin preparations of alveolar macrophage suspensions from bronchoalveolar lavages. The immunological identity of human and bovine purple phosphatases from alveolar macrophages was demonstrated by Western blot analysis of material separated by polyacrylamide gel electrophoresis. A possible significance of the purple phosphatase as a marker enzyme of activated cells of the mononuclear phagocyte system is discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 23 (1991), S. 38-42 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A tartrate-resistant acid phosphatase activity was detected in the human placenta. This enzyme displayed immunological properties similar to those of the group of purple acid phosphatases that can be demonstrated with a rabbit polyclonal antibody against bovine spleen purple acid phosphatase. The placental enzyme was mainly localized immunohistochemically to neutrophil granulocytes of the maternal blood between the placental villi and within foetal capillaries using the bovine spleen antibody and the commercial monoclonal antibody M1 directed against an antigen found on mature granulocytes. A minor activity was detected in decidual cells and the syncytiotrophoblast. The presence of purple acid phosphatase in placental granulocytes may be related to special immunological conditions of pregnancy.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0878
    Keywords: Key words: Urothelium ; Tartrate-resistant acid phosphatase ; Nitric oxide synthase I ; Superoxide dismutase ; Immunocytochemistry ; Free radicals ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Three enzymes, viz., tartrate-resistant acid phosphatase (TRAP), nitric oxide synthase I (NOS-I), and superoxide dismutase (SOD), involved in the production and metabolism of free radicals or radical equivalents, were demonstrated by immunocytochemistry in the urothelium of the ureters of six patients of various ages. Two of these enzymes (TRAP and NOS-I) were colocalized in the most apical and lateral border of the superficial cells of the urothelium. In contrast, SOD showed a patchy or granular distribution within the supranuclear region of these cells. Intra- and subepithelial macrophages exhibited a weak TRAP, but no NOS-I or SOD, immune reaction. On the basis of the immunocytochemical findings, arguments in favor of a cytotoxic function of the superficial cells of the human urothelium are presented.
    Type of Medium: Electronic Resource
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