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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Ultrasructure Research 85 (1983), S. 249-259 
    ISSN: 0022-5320
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0022-5320
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Ultrasructure Research 77 (1981), S. 210-222 
    ISSN: 0022-5320
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Cell Biology International Reports 14 (1990), S. 44 
    ISSN: 0309-1651
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 46 (1976), S. 189-196 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Male albino rats (Sprague Dawley) were fed for 2–6 weeks on a diet containing 0.75% clofibrate. Liver cell fractions obtained from these animals were assayed for peroxisomal enzymes. In the cell homogenate the catalase activity was doubled, whereas the activity of urate oxidase was found to be only slightly depressed. The activity of carnitine acetyltransferase increased several times. In liver peroxisomes purified by isopycnic gradient centrifugation the specific activity of urate oxidase decreased appreciably showing that peroxisomes formed under the proliferative influence of clofibrate are not only modified with respect to their morphological characteristics but also to their enzymic equipment. This is also obvious from the changes in peroxisomal carnitine acetyltransferase activity which was enhanced by clofibrate to more than the fivefold amount. In purified mitochondria this enzyme was even more active: clofibrate advances both, the peroxisomal and the mitochondrial moiety of carnitine acetyltransferase. Morphological and cytochemical studies showed an increase in the number of microbodies and as compared to the controls microbodies were lying in groups more frequently. Small particles located closely adjacent to “normal” sized peroxisomes were found particularly after short feeding periods. While the number of coreless microbodies increased studies gave no clear evidence for an increase in marked shape irregularities of the peroxisomes.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 43 (1975), S. 373-385 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution pattern of histochemically detectable 5′-nucleotidase (5′-Nase) activity is described in smooth muscle cells of the rat's gastrointestinal tube (esophagus, stomach, small intestine, large intestine). Both, light and electron microscopic methods are used. Faint positive 5′-Nase activity is observed on smooth muscle cells of the lamina muscularis mucosae in the thoracal esophagus whereas it is completely absent from smooth muscle cells of the abdominal esophagus and the stomach. In the small and large intestine strong positive 5′-Nase reaction is found on smooth muscle cells of the lamina muscularis mucosae and the innermost part of the lamina muscularis externa. In the circular and longitudinal layer of the lamina muscularis externa a slight increase in 5′-Nase activity is observed from the proximal to the distal segments. The reaction product is restricted to the outer cell surface of smooth muscle cells. In the small intestine the strong enzymatic activity in the innermost part of the muscularis externa is found to be localized at small and dense muscle cells (sd-cells). Common morphological and histochemical characteristics of sd-cells and smooth muscle cells of the lamina muscularis mucosae are emphasized. Hypothetical functions e.g. uptake of precursors of nucleosidephosphates, possible functional connection to a high glycogen content, correlation between 5′-Nase activity and proliferation capacity and local vasodilatory effect are discussed.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 109 (1998), S. 555-570 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The endocytic routes of labelled lectins as well as cationic ferritin were studied in cells with a regulated secretion, i.e. pancreatic beta cells, and in constitutively secreting cells, i.e. fibroblasts and HepG2 hepatoma cells, paying particular attention to routes into the Golgi apparatus. Considerable amounts of internalised molecules were taken up into the trans Golgi network (TGN) and into Golgi subcompartments in all three cell types as well as in secretory granules of the pancreatic beta cells. The internalised materials did not pass rapidly the TGN and Golgi stacks, but were still present hours after internalisation, being then particularly concentrated in TGN-elements and in the transmost Golgi cisterna. Endocytosed materials reached forming secretory granules present in the TGN. Further, direct fusion between endocytotic vesicles and mature secretory granules was observed. Golgi subcompartments as well as endocytic TGN containing endocytosed materials were in close apposition to specialised regions of the endoplasmic reticulum. The Golgi apparatus including its parts containing endocytosed materials were transformed into a tubular reticulum upon treatment with the fungal metabolite Brefeldin A. Rarely, internalised material was observed in the lumen of the endoplasmic reticulum, thus providing evidence for an endocytic plasma membrane to endoplasmic reticulum route.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 50 (1976), S. 47-55 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Brown adipose tissue of normal and cold-adapted adult rats has been investigated morphologically and cytochemically. In thin sections catalase-positive particles appear as circular, oval or elongated profiles lying either as single particles or forming groups. Biochemical studies on peroxisomal enzymes show an increase of catalase activity to the tenfold amount after cold adaptation. The tissue is devoid of D-aminoacid oxidase and glycolate oxidase, while low activities of middle-chain α-hydroxyacid oxidases could be detected. The catalase-positive particles were purified by differential and isopycnic gradient centrifugation. The density of the particles (1.20 g/cm3) is lower than that of the liver peroxisomes. Enzymic investigations of the fractions render it probable that particles contain carnitine acetyltransferase, whereas they are lacking NAD-dependent glycerophosphate dehydrogenase. The pellets derived from the gradient centrifugation have been checked morphologically for purity. After performing DAB-cytochemistry for identification of the peroxidatic activity of catalase, most of the particles were shown to be structurally intact and homogeneously filled with reaction product.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 71 (1981), S. 259-267 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Membranes of liver peroxisomes from rats fed with clofibrate were purified in a discontinuous gradient using a zonal rotor. The preparation consists of round or oval vesicles mostly devoid of nucleoids with a diameter ranging from 70–700 nm; open sheets are found very infrequently. Mitochondrial profiles as well as vesicles containing cytochemically demonstrable glucose 6-phosphatase are scarce; accordingly, glucose 6-phosphatase is nearly undetectable biochemically. Monoamine oxidase is absent in peroxisomal membranes. Cytochrome b5 is found in a concentration of 0.3 nmoles/mg protein, an order of magnitude comparable to the content of endoplasmic reticulum membranes. Reduction of this cytochrome with palmitoyl-CoA is possible only after recombination of the membranes with the soluble peroxisomal matrix fraction.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 165 (1976), S. 371-382 
    ISSN: 1432-0878
    Keywords: Tracheal epithelium, Organ culture ; Rat, mouse ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Electron microscopic studies of adult rat and mouse tracheal epithelium maintained in organ culture for a period of up to 6 days were performed. In specimens cultured for 60 minutes no conspicuous micromorphological alterations could be observed. Following culture periods from 1–6 days the number of cilia in some of the ciliated cells was reduced while their structure and the other ultrastructural details of the epithelial cells were preserved. In specimens cultured for 5–6 days some additional alterations could be noticed: polymorphism of mitochondria, increased number of lysosomes, appearance of intracellular vacuoles, exhaustion of goblet cells and disappearance of granulated mast-cell like cells in the rat tracheal epithelium. I want to thank Miss J. Selbmann and Mrs. S. Kolassa for technical help and Mr. H. Wagner for preparing the micrographs; I am indebted to Dr. D. Kerjaschki and to Mr. H. Hörandner for performing preparations for scanning electron microscopy and to Mr. P. Scholze (Österreichische Studiengesellschaft für Atomenergie, Institut für Metallurgie, Abteilung Fremdkörperphysik) for preparing the scanning electron micrograph.
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