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  • Electronic Resource  (2)
  • Chicken  (1)
  • Secretion  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 107 (1970), S. 403-420 
    ISSN: 1432-0878
    Keywords: Parotid ; Peroxidase ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Die Lokalisation endogener Peroxydase wurde in der Glandula parotis der Ratte mit der Methode von Graham und Karnovsky (1966) untersucht. Lichtmikroskopisch ist das Reaktionsprodukt im basalen Cytoplasma, in den Sekretgranula und, nach Pilocarpinreizung, in den Lumina der interzellulären Sekretkapillaren, der Drüsenendstücke und der Schaltstücke nachweisbar. Der Speichel enthält eine Peroxydase, die durch Hitze (100°) und durch KCN und 3-Amino-1,2,4-Triazol hemmbar ist. Der Speichel zeigt bei 415 mμ eine Schulter im Absorptionsspectrum, die nach Komplexbildung mit H2O2 um 15 mμ nach rechts verschoben wird. Elektronenmikroskopisoh läßt sich das Reaktionsprodukt der Peroxydase in allen Cisternen des rauhen endoplasmatischen Reticulums, einschließlich der perinucleären Cisterne, in glattwandigen Bläschen zwischen rauhem endoplasmatischen Reticulum und Golgi-Membranstapeln, in den kondensierenden Vacuolen und in allen Sekretgranula nachweisen. Die Cisternen des Golgi-Apparates enthalten selten Reaktionsprodukt. In der Glandula parotis der Ratte sind vorwiegend die kondensierenden Vacuolen, in geringerem Maße auch die Cisternen des Golgi-Apparates, an der Segregierung und Kondensierung von Peroxydase beteiligt.
    Notes: Summary The localization of endogenous peroxidase was investigated in the parotid gland of the rat by the method of Graham and Karnovsky (1966). By light microscopy, the reaction product was localized in the basal cytoplasm, in secretion granules, and, after injection of pilocarpine hydrochloride, in the lumina of the intercellular canaliculi, the acini and the intercalated ducts. The peroxidase reaction of the saliva collected from the oral cavity can be suppressed by heat (100° C), by 3-amino-1,2,4-triazole, and by KCN. Absorption spectra of the saliva show a shoulder at 415 mμ which is shifted by 15 mμ towards longer wave lengths after complexing with H2O2. At the ultrastructural level, reaction product is present in all cisternae of the rough endoplasmic reticulum including the perinuclear cisternae, in smooth vesicles located between the rough endoplasmic reticulum and the stacks of Golgi cisternae, in condensing vacuoles, and in all secretion granules. The Golgi cisternae seldom contain reaction product. The results show that in the parotid gland of the rat, the condensing vacuoles and, to a lesser extent, the cisternae of the Golgi apparatus function in the segregation and condensation of peroxidase.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 252 (1988), S. 349-358 
    ISSN: 1432-0878
    Keywords: Thyroglobulin ; Sulfation ; Thyroid gland ; Vertebrates ; Evolution ; Trout (Salmo gairdnerii) ; Clawed toad (Xenopus laevis) ; Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Mammalian thyroglobulin is released by thyroid follicle cells as a sulfated glycoprotein; the sulfate residues are mostly linked to tyrosine, but they are also attached to the high-mannose carbohydrate side-chains. To decide whether sulfation of thyroglobulin is confined to mammals, representatives of other vertebrate classes were analyzed for the presence of sulfated thyroglobulin: fish (trout), amphibians (clawed toad) and birds (chicken). Mini-organs were prepared from thyroid tissue and suspended in a 35SO 4 -- -containing culture medium. Light- and electron-microscope autoradiographs prepared from the mini-organs showed that thyroid follicle cells from all species examined incorporate 35SO 4 -- and synthesize a sulfated secretory product which accumulates in the follicle lumen. The Golgi complex was detected as the primary intracellular site of sulfate organification. The 35SO 4 -- -radiolabeled secretory product of all species was shown by polyacrylamide-gel-electrophoretic analyses to consist of thyroglobulin, identified by comparison with biosynthetically 125I-labeled thyroglobulin. The results indicate that the sulfation of thyroglobulin is a ubiquitous post-translational modification observed already in the thyroglobulin of lower vertebrates. Our observations suggest that sulfation of thyroglobulin was acquired in the early stages of thyroid evolution.
    Type of Medium: Electronic Resource
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