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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 3 (1970), S. 210-222 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Cyanide (CN) and dinitrophenol (DNP) rapidly depolarize the cells of oat coleoptiles (Avena sativa L., cultivar Victory) and of pea epicotyls (Pisum sativum L., cultivar Alaska); the effect is reversible. This indicates that electrogenesis is metabolic in origin, and, since active transport is blocked in the presence of CN and DNP, perhaps caused by interference with ATP synthesis, that development of cell potential may be associated with active ion transport. Additional evidence for an electrogenic pump is as follows. (1) Cell electropotentials are higher than can be accounted for by ionic diffusion. (2) Inhibition of potential, respiration, andactive ion transport is nearly maximal, but a potential of −40 to −80 mV remains. This is probably a passive diffusion potential since, under these conditions, a fairly close fit to the Goldman constant-field equation is found in oat coleoptile cells.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Na+, K+-ATPase ; Immunocytochemistry ; Kidney ; Salivary glands ; Transport ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An antibody to the 96 kD α-subunit of the Na+, K+ -ATPase from Bufo marinus has been used in immunostaining rat kidney and salivary glands. Intense staining was observed on basolateral membranes of distal tubules of the kidney and striated ducts of the three major salivary glands. Less intense staining was seen on the basolateral membranes of parotid acinar cells, but no staining was seen on the acinar cells of submandibular or sublingual glands. These sites of staining have been shown, by other methods, to posses substantial Na+, K+ -ATPase, indicating that the antibody recognizes antigenic determinants of the sodium pump highly conserved in the course of evolution. In addition, staining with this antibody was observed at the apical region of cells of the proximal straight tubule and of the papillary collecting duct in the kidney. Absorption studies suggest that the apical antigenic determinants are the same or closely related to each other but are distinct from basolateral antigenic determinants.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular histology 15 (1983), S. 239-255 
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The diuretic compound amiloride is often used as a specific inhibitor of the passive Na+ entry step in the transepithelial transport of Na+ across frog skin. We have utilized the fluorescence properties of amiloride to study the distribution of this transport inhibitor in the ventral skin ofRana pipiens. After a 30 s exposure of 1–100 μm amiloride to the external surface of frog skin, amiloride fluorescence was evident in the cytoplasm of all cell layers of the epidermis and alveolar gland epithelium. Changes in the conditions of incubation which alter the pharmacological activity of amiloride did not affect the intracellular distribution of amiloride or the washout profile of [14C]amiloride. The presence of amiloride fluorescence in the cytoplasm prevented our examination of changes in the amiloride fluorescence at the cell surface with various conditions of incubation. Four derivatives of amiloride that differed in their ability to inhibit short-circuit current were also localized intracellularly but varied in their relative distribution among the cell layers of the epidermis. Our results indicate that when incubated at concentrations from 1 to 100 μm, a large fraction of the amiloride taken up by frog skin is not directly involved with the inhibition of passive Na+ transport at the apical surface of the stratum granulosum. The mechanism of intracellular uptake of amiloride is not clear. However, the cytoplasmic localization of amiloride could explain the action of the drug on intracellular enzymes and may account for the large proportion of non-displaceable [14C]amiloride that has been observed in frog skin.
    Type of Medium: Electronic Resource
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  • 4
    Publication Date: 1998-12-15
    Print ISSN: 0163-1829
    Electronic ISSN: 1095-3795
    Topics: Physics
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