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  • 11
    Electronic Resource
    Electronic Resource
    Theory for interfacial tension of partially miscible liquids
    Amsterdam : Elsevier
    Physica A: Statistical Mechanics and its Applications 179 (1991), S. 219-231 
    Details
    ISSN: 0378-4371
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-4371(91)90060-P
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  • 12
    Electronic Resource
    Electronic Resource
    Statistical mechanics basis of Macleod's formula (1990)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 94 (1990), S. 8362-8364 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100384a068
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  • 13
    Electronic Resource
    Electronic Resource
    Distribution of acid hydrolases in the nephron of normal and diabetic rats
    Amsterdam : Elsevier
    International Journal of Biochemistry 12 (1980), S. 41-45 
    Details
    ISSN: 0020-711X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0020-711X(80)90039-7
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  • 14
    Electronic Resource
    Electronic Resource
    The activity pattern of two peroxisomal oxidases in the rat rephron
    Amsterdam : Elsevier
    FEBS Letters 127 (1981), S. 253-256 
    Details
    ISSN: 0014-5793
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(81)80217-7
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  • 15
    Electronic Resource
    Electronic Resource
    5′-Nucleotidase in spinal meningeal compartments in the rat (1992)
    Springer
    Histochemistry and cell biology 98 (1992), S. 135-139 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of 5′-nucleotidase (5′-Nu) is reported in spinal meninges of the rat on the basis of an immunohistochemical and enzyme histochemical investigation. Strong immunoreactivity was found in the arachnoid membrane and in the sheaths of the spinal roots as well as in septa subdividing the roots. Also the superficial layer of the ligamentum denticulatum showed enzyme staining. No immunoreactivity could be detected in the pia mater or along the spinal nerve roots outside the subarachnoid space. Within the arachnoid mater the immunoreactivity was concentrated in the basal zone of the arachnoid membrane, thus appearing as a narrow fluorescent band near the border of the dura. An accentuation of immunoreactivity could be observed in areas where small dural blood vessels approach the subarachnoid space. It is well known that adenine nucleotides released from neural and glial cells of the central nervous system finally reach the cerebrospinal fluid. We presume that 5′-Nu in the arachnoid membrane and spinal root sheaths is responsible for the conversion of adenine nucleotides into adenosine and that this conversion is associated with the reabsorption process of cerebrospinal fluid which most probably also takes place in spinal meninges. Adenosine, the product of 5′-nucleotidase, could play a role in the reabsorption process by its vasodilatatory effect on dural and epidural vessels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00717005
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  • 16
    Electronic Resource
    Electronic Resource
    Localization of nucleotide pyrophosphatase in the rat kidney (1986)
    Springer
    Histochemistry and cell biology 86 (1986), S. 207-210 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Hydrolysis of NAD by a nucleotide pyrophosphatase of renal membrane fractions has been reported previously. The aim of the present study was to localize this enzyme in the rat kidney. Nucleotide pyrophosphatase was assayed in glomeruli, in three parts of the proximal tubule and in four parts of the distal tubule dissected form freezedried sections. Nucleotide pyrophosphatase activity, expressed in μmol·min−1·mg protein−1, ranged between 9.8 and 32.3 in the proximal tubular segments and between 1.1 and 2.7 in the distal tubular segments. It was 3.4 in the glomeruli. The enrichement of the activity during the purification of brush border vesicles was measured. A tenfold higher specific activity was found in the brush border vesicles as compared to the renal cortical homogenates. Thus, most of the renal nucleotide pyrophosphatase appears to be localized in the luminal membrane of the proximal tubule. A permeabilization of the membrane did not increase the activity of brush border vesicles. This indicates that all catalytic sites are accessible at the outer surface of the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493389
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  • 17
    Electronic Resource
    Electronic Resource
    Distribution of ecto-5′-nucleotidase in the rat liver: effect of anaemia (1994)
    Springer
    Histochemistry and cell biology 101 (1994), S. 439-447 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In the kidney a striking parallel exists between the expression of ecto-5′-nucleotidase and of erythropoietin by renal fibroblasts. It was therefore hypothesized that the expression of ecto-5′-nucleotidase in fibroblasts might be controlled by oxygen tension. In order to test this hypothesis, we examined the distribution of the enzyme in a tissue which displays a defined zonation in respect to oxygen tension, namely in the liver; anaemia was used in order to exaggerate this zonation. The distribution of ecto-5′-nucleotidase was investigated by light and electron microscopy using enzyme and immunohistochemical methods in the livers of healthy and of anaemic rats. Anaemia was produced by haemolysis combined with X-ray irradiation. The enzyme was detected in the bile canaliculi, in the connective tissue of the portal triads and of the central veins, and in fat-storing cells probably corresponding to a special form of fibroblasts. In healthy animals the perisinusoidal ecto-5′-nucleotidase activity was slightly higher in the pericentral than in the periportal area of the acinus whereas the inverse was observed for the staining of bile canaliculi. Anaemia provoked an increase of ecto-5′-nucleotidase in fat-storing cells in the pericentral zone of the acinus and in fibroblasts around the central veins, resulting in steepended gradients along the sinusoids. The intralobular gradient of ecto-5′-nucleotidase in perisinusoidal cells and the effect thereon of anaemia suggest that the expression of the ecto-5′-nucleotidase might be directly or indirectly controlled by local oxygen tension.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269494
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  • 18
    Electronic Resource
    Electronic Resource
    Ecto-5′-nucleotidase is expressed by pericytes and fibroblasts in the rat heart (1995)
    Springer
    Histochemistry and cell biology 103 (1995), S. 227-236 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Ecto-5′-nucleotidase is anchored at the outer surface of cell membranes and thus its reaction product adenosine is released into the extracellular space. Extracellular adenosine displays via specific receptors a wide range of physiological effects in heart. There are discrepancies in the literature concerning the distribution of ecto-5′-nucleotidase in heart. Since we suspected that these may be due to technical problems, in the present study on ecto-5′-nucleotidase in rat heart we attempted to circumvent some technical pitfalls. Good preservation of the tissue with open capillary lumina, providing a clear identification of endothelium, was obtained by perfusion fixation. At the light microscopic level, the distribution of ecto-5′-nucleotidase studied by enzyme histochemistry and immunohistochemistry using a monoclonal and a polyclonal antibody yielded congruent results. The enzyme was rather homogeneously distributed throughout the myocardium, with a slightly higher incidence of stained cells in the outer thirds than in the inner third of the wall. Consistently high levels of ecto-5′-nucleotidase were seen only in interstitial cells. The walls of large vessels and heart muscle cells were constantly negative for ecto-5′-nucleotidase. The endothelia of capillaries were mostly negative but a few profiles occasionally displayed a weak immunoreaction. The interstitial cells staining positive for ecto-5′-nucleotidase could be identified as pericytes and as fibroblasts according to their shapes and localizations. The immunoreactivity of fibroblasts was confirmed by electron microscopy. These data indicate that adenosine may be formed extracellularly in the interstitium of the myocardium, where it would have direct access to important targets such as myocytes, arterioles and nerve endings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01454028
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  • 19
    Electronic Resource
    Electronic Resource
    Quantitative distribution of lysosomal hydrolases in the rat nephron (1979)
    Springer
    Histochemistry and cell biology 63 (1979), S. 245-251 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The activities of N-acetyl-β,d-glucosaminidase (NAG, EC 3.2.1.30),β,d-galactosidase (β-gal, EC 3.2.1.23) and acid phosphatase (ac-Pase, EC 3.1.3.2) were measured in the glomeruli, five segments of the proximal and four segments of the distal tubule of normal male Wistar rats. The activities of NAG andβ-gal are 3- to 5-fold higher in the first part of the proximal tubule than in other segments and very low in glomeruli. We propose that the distribution of these two glycosidases reflects the contribution of the different tubular segments to the reabsorption of glycoproteins. The maximal activity of ac-Pase was found in the straight part of the proximal tubule. It was only 1.5-fold higher than in the distal tubule. Moreover, the activity in glomeruli is rather high. We conclude that ac-Pase is not primarily involved in the handling of reabsorbed molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00644546
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  • 20
    Electronic Resource
    Electronic Resource
    The activities of peroxisomal oxidases in periportal and perivenous zones of the rat liver acinus (1980)
    Springer
    Histochemistry and cell biology 69 (1980), S. 95-99 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using a new biochemical microassay the activities of three peroxisomal oxidases in single microdissected periportal and perivenous zones of the liver acinus were measured. Whereas urate oxidase is homogeneously distributed through the acinus, the activities of D-aminoacid oxidase and α-hydroxyacid oxidase are respectively 1.80-and 2.71-fold higher in the periportal hepatocytes than in the perivenous hepatocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00508370
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