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  • Articles: DFG German National Licenses  (17)
  • 11
    Electronic Resource
    Electronic Resource
    Studies on mouse liver urate oxidase (1973)
    Springer
    Histochemistry and cell biology 36 (1973), S. 21-27 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of urate oxidase in mouse liver was investigated by fluorescent antibody technique. The fluorescence was observed in the cytoplasm and fine granules scattering throughout the cytoplasm of liver cells. The diffuse cytoplasmic fluorescence around the central vein was somewhat stronger than that of the medial and outer zone of hepatic lobule. Nuclei of the liver cell and stellate cell of Kuppfer were not stained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310117
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  • 12
    Electronic Resource
    Electronic Resource
    Enzyme cytochemical localization of sarcosine oxidase activity in the liver and kidney of several mammals (2000)
    Springer
    Histochemistry and cell biology 113 (2000), S. 489-495 
    Details
    ISSN: 1432-119X
    Keywords: Enzyme cytochemistry Sarcosine oxidase Peroxisomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We investigated the enzyme cytochemical localization of sarcosine oxidase (SOX) in the liver and kidney of several mammals using a cerium technique. First we measured the enzyme activities in the liver and kidney of several mammals and in several organs of mice. The highest activity was found in the Chinese hamster, followed by the mouse. Therefore, we used hamster and mouse tissues for enzyme cytochemistry. The liver and kidneys were fixed by perfusion with various concentrations of glutaraldehyde for 10 min. Tissue slices were incubated in reaction medium consisting of 50 mM TRIS-maleate buffer (pH 7.8), 9 mM sodium azide, 9.8 mM sarcosine, 25 µM FAD, 2 mM cerium chloride, 0.002% saponin, and 0.003% Triton X-100 for 0.5–8 h at 37°C. Optimum staining reaction was obtained in tissues fixed with 0.2% glutaraldehyde, followed by incubation for 2–4 h. Electron-dense reaction products were present exclusively in peroxisomes. Within the peroxisomes strong reactions were observed in the matrix subjacent to the limiting membrane decreasing toward the center. The staining reaction was completely inhibited by 2 mM N-bromosuccinimide. These results indicated that SOX is a peroxisomal enzyme and that the enzyme might be associated with the peroxisomal membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180000161
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  • 13
    Electronic Resource
    Electronic Resource
    Electron microscopic localization of carbonic anhydrase (CA) activity in rabbit cornea (1975)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 197 (1975), S. 145-152 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Lokalisation der Carboanhydrase-Aktivität wurde bei Kaninchenhornhäuten mit einer modifizierten Methode nach Hansson untersucht. Spezifische Reaktionsprodukte konnten an den seitlichen Zellmembranen des Endothels beobachtet werden. Im Cytoplasma, im Golgikomplex und in den Mitochondrien waren keine spezifischen Ablagerungen zu finden, ebensowenig im Epithel, im Stroma und in der Descemetschen Membran. Bei einer Kontrollgruppe ließ sich die spezifische Färbung mit 10−4 M Azetazolamid hemmen.
    Notes: Summary The localization of CA activity in the rabbit cornea was investigated using a modified Hansson's method. The reaction products indicating CA activity were observed in the lateral membrane of endothelial cell, but not in the apical membrane. In cytoplasm, Golgi complex, and mitochondria of the endothelial cells no specific reaction product could be found. In epithelium, stroma, and Descemet's membrane, no reaction product was seen. The specific staining was inhibited in the control group which was treated with 10−4 M sodium acetazolamide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02388780
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  • 14
    Electronic Resource
    Electronic Resource
    Licht- und elektronenmikroskopische Untersuchungen an kurzzeitkonservierten Hornhäuten (1976)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 199 (1976), S. 121-131 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Kaninchenhornhäute wurden mit einem Sklerarand von Bulbus abpräpariert und in verschiedenen Medien bei +4°C konserviert: in 5% Dextran T 40, in McCoy's 5a Medium (modified), in 5% Dextran T 40+ McCoy's 5a Medium, in Dextran 5% T 40+ McCoy's 5a Medium + Gentamycinsulfat (250 μg/ml). Das Hornhautendothel wurde nach 1, 6, 12 und 18 Tagen licht- und elektronenmikroskopisch untersucht und verglichen mit dem Endothel frischer Kaninchenhornhäute und mit dem Hornhautendothel von Bulbi, die in feuchter Kammer bei +4°C gelagert waren. Die Untersuchungen zeigten, daß noch eine 6-tägige Lagerung der Hornhäute in 5% Dextran T 40+ McCoy's 5a Medium mit Refobacin® gute Voraussetzungen für eine erfolgreiche Keratoplastik bietet.
    Notes: Summary Rabbit corneae were stored at a temperature of +4°C in the following media: 1. 5% Dextran T40, 2. McCoy's Medium 5a (modified), 3. Dextran T40+Mc Coy's 5a Medium + gentamicin sulphate (250 μg/ml). The endothelia of the corneae were examined by light and electron microscopy after preservation for a varied number of days. The structure of the endothelia, stored for 1, 6, 12, 18 days, was compared to fresh corneal endothelial cells. The results indicate that corneae preserved in Dextran 5% T 40 + McCoy's 5a Medium + gentamicin sulphate might be equivalent to fresh corneal tissue in keratoplasties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02385208
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  • 15
    Electronic Resource
    Electronic Resource
    Cytochemical localization of nucleoside diphosphatase and thiamine pyrophosphatase activities in the rabbit corneal endothelium (1977)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 202 (1977), S. 45-54 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Lokalisation der Nucleosiddiphosphatase (NDPase) und der Thiaminpyrophosphatase (TPPase) im Endothel der Kaninchenhornhaut wurde histochemisch untersucht. Nach Inkubation bei pH 7.0 und 8.0 konnte die NDPase-Aktivität in den Cisternen des endoplasmatischen Reticulums gefunden werden, außerdem in der Kernmembran und in den Sacculi des Golgi-Komplexes. Die TPPase-Aktivität konnte lediglich in den Sacculi des Golgi-Apparates entdeckt werden. Die Reaktionsprodukte beider Enzyme waren bei pH 8.0 vermindert. Die NDPase-Aktivität wurde durch Uranylnitrat gehemmt, jedoch nicht durch Natriumfluorid, während die TPPase durch Natriumfluorid, aber nicht durch Uranylnitrat gehemmt wurde.
    Notes: Summary Localization of NDPase and TPPase activities in the rabbit corneal endothelium was investigated by cytochemical methods. After incubation at both pH 7.0 and 8.0, the NDPase activity was detected in cisternae of ER, nuclear envelope, and Golgi saccules, while the TPPase activity was demonstrated only in Golgi saccules. The reaction products of both enzymes were decreased when incubated at pH 8.0. The NDPase activity was inhibited by uranyl nitrate but not by sodium fluoride, while the TPPase was inhibited by fluoride but not by uranium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496767
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  • 16
    Electronic Resource
    Electronic Resource
    Involvement of cathepsins B and H in lysosomal degradation of horseradish peroxidase endocytosed by the proximal tubule cells of the rat kidney: I. Histochemical and immunohistochemical studies (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 221 (1988), S. 783-790 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Immunohistochemical localizations of horseradish peroxidase (HRP) and cathepsins B and H in the lysosomal system of the rat kidney proximal tubule cells were investigated during the internalization and degradation of HRP by these cells. At fixed intervals after intravenous injection of HRP, the kidneys were fixed by perfusion. Five to fifteen minutes after this injection, endocytosed HRP was detected in fine granules beneath the brush border. Thirty minutes later, it accumulated into large aggregates of granules (phagosomes), where both enzymatic and antigenic activities appeared to cause HRP to be lost rapidly. After 1 hour, the aggregates of phagosomes increased in number and size but soon began to decrease gradually. In the early stage, cathepsins B and H were not detected in the apical cytoplasmic granules. However, they were present in the lysosomal compartments, together with the HRP. The large aggregates of phagosomes showed a patchy reaction, especially approximately 30 minutes after injection, whereas other medium-sized phagosomes were stained heavily. Aggregates of phagosomes were present only in the S1 segment. These results suggest strongly that cathepsins B and H are involved in the cellular degradation of endocytosed HRP.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092210402
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  • 17
    Electronic Resource
    Electronic Resource
    Involvement of cathepsins B and H in lysosomal degradation of horseradish peroxidase endocytosed by the proximal tubule cells of the rat kidney: II. Immunocytochemical studies using protein A-gold technique applied to conventional and serial sections (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 221 (1988), S. 791-801 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Immunoelectron microscopic localizations of cathepsins B and H and injected horseradish peroxidase (HRP) in the lysosomal system of rat kidney proximal tubules were investigated by a protein A-gold technique. Kidneys were fixed by perfusion at fixed intervals after intravenous injection of HRP. At 5 to 15 minutes after the injection, the endocytic apparatus - including the apical vesicles, tubules, and vacuoles (endosomes) - were stained for HRP, but they were negative for cathepsins. Within 15 to 30 minutes after the HRP injection, HRP-containing endosomes were fusing with preexisting lysosomes. In the S1 segment, they accumulated in the apical cytoplasm and formed giant phagosomes, which increased markedly in number and size after 1 hour. These phagosomes were composed of a peripheral clear matrix and electron-dense inclusions. The clear matrix was stained heavily for cathepsins and HRP, whereas the electron-dense inclusions were consistently negative for cathepsins and HRP. The same results also were obtained after the double-labeling and serial sectioning techniques. The dense inclusions were fragmented gradually as the phagosomes decreased in size. After 3 hours, the size and number of phagosomes returned to their normal state (before the HRP injection). These results indicate that the endocytic apparatus of the proximal tubule cells does not contain cathepsins. Phagosomes are formed by the fusion of endosomes containing the internalized protein with the preexisting lysosomes. The degradation of HRP in giant phagosomes occurred rapidly. The coexistence of cathepsins B and H with the endocytosed HRP suggests that these cystein proteinases are involved in the degradation of protein in heterophagosomes of the proximal tubule cells.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092210403
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