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  • 1
    ISSN: 1432-0568
    Keywords: Key words Morphogenesis ; Histochemistry ; Lectins ; Carbohydrates ; Salivary glands ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The developmental expression of salivary glycoconjugates was investigated in the rat submandibular and sublingual glands by conventional and lectin histochemistry. By the time of the first differentiation of secretory structures, in spite of similar morphological features, a different histochemical reactivity was detected, accounting for a relevant content of neutral glycoconjugates in the submandibular gland and the occurrence of both neutral and acidic glycoconjugates in the sublingual one. The use of lectins allowed the main changes of secretory components to be noted around gestational day 18. DBA and WGA lectins seemed to act as pre- and post-natal development markers while Con A lectin was indicative of post-natal differentiation. Taken together, data from lectin histochemistry indicated the transitional occurrence of glycoconjugates, probably involved in temporally restricted functions, as well as the co-existence of different secretory components that might also reflect maturational changes of single products.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 183 (1991), S. 41-48 
    ISSN: 1432-0568
    Keywords: Carbonic anhydrase ; Mesonephros ; Quail ; Development ; Regression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Carbonic anhydrase activity was studied during development and regression of the quail mesonephros by in situ and extra situm investigation. A close correlation was noted between enzyme expression and tissue morphofunctional state. Carbonic anhydrase appears in early development; its highest activity is reached when the kidney is actively secreting, followed by a decrease concomitant with tissue involution. The main localization of the reaction product is the distal tubule showing strongly positive cells intercalated with clear, negative ones. In the functional organ, staining was found at the level of transitional and connecting segments and Wolffian duct. The comparison with the histochemical pattern of the quail metanephros suggests that the functional meaning of renal carbonic anhydrase might be the same both in transitory and in permanent kidney.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 37 (1981), S. 409-411 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Carbonic anhydrase (CA) activity has been localized histochemically by Hansson's method in Malpighian tubules ofCulex pipiens. The enzyme has been observed on membranes of the cytoplasmic inclusions of Malpighian cells; no CA activity has been found in other cytoplasmic structures. The possible meaning of the localization of the enzyme is discussed.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effects of different concentrations of acetazolamide, a specific carbonic anhydrase inhibitor, have been investigated in the quail kidney. The histochemical patterns, interpreted by means of quantitative analyses proved that 0.1 μm acetazolamide inhibited the enzyme activity in all the reactive tubular segments except for distal tubules. At this site, the reaction product disappeared from the cytoplasm but strong positivity persisted at the apical surface. The luminal staining was still present at higher inhibitor concentrations up to 0.8 μm acetazolamide. Under histophotometric analyses, the residual reactivity proved to be nearly the same at the increasing inhibitor concentrations assayed. The validity of the results was checked by similar investigations in other control tissues. On the basis of the properties known for carbonic anhydrase in mammalian kidney, we conclude that the luminal membrane staining in the quail distal tubules might be due to a carbonic anhydrase isoenzyme that is similar, both in affinity for acetazolamide and in intracellular localization, to the membrane-bound enzyme purified from mammalian proximal convoluted tubules.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The immunohistochemical localization of carbonic anhydrase isoenzymes has never been investigated in avian renal tissue previously. Enzyme activity has largely been documented by histochemical and physiological reports. In this investigation, specific antisera were used to study the distribution of the cytosolic carbonic anhydrase II and III isoenzymes in the quail kidney. Comparison between the present findings and the corresponding histochemical patterns, previously obtained in the same species by a cobalt phosphate precipitation method, resulted in the bulk of renal carbonic anhydrase activity being attributed to the carbonic anhydrase II isoenzyme. Conversely, moderate carbonic anhydrase III immunostaining appeared to be confined to the smooth muscle cells of ureteral and arteriolar walls. Indirect evidence of the occurrence, in the quail kidney, of a membrane-associated carbonic anhydrase form, antigenically distinct from the II and III isoforms, was inferred.
    Type of Medium: Electronic Resource
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