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  • 1995-1999  (3)
  • 1
    ISSN: 1432-0568
    Schlagwort(e): Key words Morphogenesis ; Histochemistry ; Lectins ; Carbohydrates ; Salivary glands ; Rat
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1573-6865
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 488-496 
    ISSN: 1059-910X
    Schlagwort(e): Lectins ; Ampulla ; Isthmus ; Rabbit ; HCG ; Estradiol ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Allgemeine Naturwissenschaft
    Notizen: Localization of individual glycosidic residues and sialic acid acceptor sugars was investigated by conjugated lectins in the rabbit oviduct under physiological hormonal conditions and human chorionic gonadotropin (HCG) administration. Ampulla and isthmus were found to exhibit lectin binding profiles typical of each hormonal stage. Two different sialylated glycomolecules were identified within the epithelial lining; in particular, sialoglycoconjugates characterized by the terminal sequence sialic acid-galactose were visualized in the secretory cells and the sialic acid-N-acetylgalactosamine terminal disaccharides were localized on both ciliated and secretory cells of the entire oviduct. Surface and cytoplasmic sialoglycoconjugates were also found to exhibit a differential behaviour inside the two oviduct tracts examined. Present findings further supported the idea that in ampulla and isthmus, the greatest modifications consequent to hormone treatment take place at different times. © 1995 Wiley-Liss, Inc.
    Zusätzliches Material: 18 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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