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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 15 (1976), S. 4279-4285 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 15 (1976), S. 4286-4292 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 75 (1953), S. 466-470 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 110 (1963), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 23 (1961), S. 37-70 
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 435 (1984), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 108 (1989), S. 177-186 
    ISSN: 1432-1424
    Keywords: Na,K-ATPase isoforms ; Artemia salina ; brine shrimp ; fluorescein isothiocyanate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Partially purified Na,K-ATPase from whole nauplii at various stages of development, analyzed by SDS-PAGE, reveals a polydisperse β and two α subunits (denoted α1 and α2). In the absence of Ca2+, ATP-inhibitable fluorescein isothiocyanate (FITC) labeling is restricted to the α subunit of this enzyme, even in crude naupliar homogenates. The intensity of the α-specific fluorescent signal (i.e., the sum of the yield from both α isoforms) is proportional to Na,K-ATPase activity during development. FITC-labeled subunits were detected at 8 hr of development prior to the detection of measurable Na,K-ATPase activity. The α2/α1 ratio changed from an initial value of 1.25 to a peak of 1.75 at 32 hr of development, then reverted to a ratio of 1.25 by 42 hr, and remained constant thereafter. Pulse chase studies with35S-methionine indicated that the developmental increase in enzyme activity is coincident with amino acid incorporation into the α subunits, implying that enzyme synthesis is active during enzyme accumulation.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 1 (1969), S. 144-176 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Studies were carried out on the morphological and physiological effects of the binding of poly-L-lysine (polylysine; mol wt≊120,000) to the apical surface membrane of the toad bladder epithelium. Paired hemibladders were mounted in chambers and exposed to polylysine concentrations of 2, 8, or 80 μg/ml in the mucosal medium for periods of up to 2 hr. Radioautographs prepared after addition of3H-polylysine showed that the polymer was localized to the apical surface of the epithelium and in dense subapical masses in lysed cells. No significant morphological changes were seen in the epithelium by light or electron microscopy at polymer concentrations of 2 and 8 μg/ml. Exposure to 80 μg/ml lysed many epithelial cells, i.e., converted them to slightly swollen ghosts with pycnotic nuclei and empty cytoplasm, except for remnants of mitochondria and vesicular fragments of the endoplasmic reticulum. All of the superficial epithelial cells were lysed in stretched hemibladders. The plasma membranes of the lysed cells were uniformly thickened, and their intercellular attachments remained intact. In contracted hemibladders, lysed and normal-appearing cells were interspersed, and the number of lysed cells in the epithelium was proportional to the duration of exposure to high concentrations of the polycation. In parallel experiments, the effects of varying concentrations of polylysine on active Na+ transport and osmotic flow of water were measured with and without vasopressin, aldosterone, or amphotericin B in the media. At a concentration of 2 μg/ml of polylysine in the mucosal bathing solutions, no change in the basal rate of Na+ transport was seen, and the response to vasopressin was unimpaired. At a concentration of 8 μg/ml, there was a significant but small fall in electrical potential difference (PD) and in short-circuit current (SCC) and no interference with the response to vasopressin. At a concentration of 80 μg/ml, there was a rapid curvilinear fall in SCC to 54±4% of the baseline value and in PD to 21±3% of the baseline value in a 2-hr period. Simultaneous unidirectional isotope flux studies with22Na and24Na showed a more than twofold increase in the serosal to mucosal flux but no discrepancy between net flux and SCC. Despite the inhibitory action of the polymer, the stimulatory response in Na+ transport to vasopressin, aldosterone, and amphotericin B was relatively preserved in that the percentage increase in SCC was the same in the polymer-treated and control hemibladders. The polycation produced a small but significant increase in osmotic water flow, and striking and irreversible inhibition of the water-flow response to vasopressin.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 108 (1989), S. 187-195 
    ISSN: 1432-1424
    Keywords: Na,K-ATPase isoforms ; Na,K-ATPase kinetics ; Artemia salina ; brine shrimp ; fluorescein-isothiocyanate ; salt glands ; intestines ; ouabain inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary To characterize the molecular properties conveyed by the isoforms of the α subunit of Na,K-ATPase, the two major transepithelial transporting organs in the brine shrimp (Artemia salina), the salt glands and intestines, were isolated in pure form. The α isoforms were quantified by ATP-sensitive fluorescein isothiocyanate (FITC) labeling. The salt gland enzyme exhibits only the α1 isoform, whereas the intestinal enzyme exhibits both the α1 and the α2 isoforms. After 32 hours of development, Na,K-ATPase activity [in μmol Pi/mg protein/hr (1u)] in whole homogenates was 32±6 in the salt glands and 12±3 in the intestinal preparations (mean±sem). The apparent half-maximal activation constants (K 1/2) of the salt gland enzyme as compared to the intestinal enzyme were 3.7±0.6mm vs. 23.5±4mm (P〈0.01) for Na+, 16.6±2.2mm vs. 8.29±1.5mm for K+ (P〈0.01), and 0.87±0.8mm vs. 0.79±1.1mm for ATP (NS). The apparentK i's for ouabain inhibition were 1.1×10−4 m vs. 2×10−5 m, respectively. Treatment of whole homogenates with deoxycholic acid (DOC) produced a maximal Na,K-ATPase activation of 46% in the salt gland as compared to 23% in the intestinal enzyme. Similar differences were found with sodium dodecyl sulfate (SDS). The two distinct forms of Na,K-ATPase isolated from the brine shrimp differed markedly in three kinetic parameters as well as in detergent sensitivity. The differences inK 1/2 for Na+ and K+ are more marked than those reported for the mammalian Na,K-ATPase isoforms. These differences may be attributed to the relative abundances of the α subunit isoforms; other potential determinants (e.g. differences in membrane lipids), however, have not been investigated.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 125 (1992), S. 163-170 
    ISSN: 1432-1424
    Keywords: serum ; low K+ ; Na,K-ATPase ; Na/K pump ; proto-oncogenes ; c-fos ; c-myc ; c-jun ; c-ski
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Cultured ARL15 cells respond to abnormally low extracellular K+ concentrations by increasing the abundance of Na,K-ATPase (the Na/K pump). This response is preceded by significant increases in the mRNAs of the α1 and β1 subunits of this enzyme, implying transcriptional or post-transcriptional regulation in the response. The present study concerned the possible participation of serum factors in low K+ induction of Na,K-ATPase. In normal K+ (4.5 mm) or low K+ (0.68 mm) the presence of 10% calf serum had no effect on Na,K-ATPase activity. The serum independence of the response to low K+ raised the possibility that low K+ may itself elicit a “growth” response. Accordingly, the effect of low K+ on mRNA abundances of four protooncogenes (c-fos, c-myc, c-jun and c-ski) was evaluated in the early phase of the response by quantitative Northern blot analysis. The mRNA for c-fos was transiently elevated by low K+, with a peak at 30 min. In contrast, low K+ had no measurable effect on the abundances of c-myc, c-jun and c-ski, for up to 2 hr of exposure. The early elevation of c-fos mRNA makes it a candidate mediator in this signal-transduction pathway. Induction of c-fos mRNA by the phorbol ester, PMA, or by dioctanoyl glycerol, however, had no effect on Na,K-ATPase activity. These results indicate that an increase in c-fos mRNA alone is not sufficient to induce Na,K-ATPase. Whether induction of c-fos is necessary for the response to low K+ remains to be determined in future studies.
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