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  • 1
    Electronic Resource
    Electronic Resource
    Bacterial phosphoenolpyruvate-dependent phosphotransferase system: association state of membrane-bound mannitol-specific enzyme II demonstrated by radiation inactivation (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 6689-6696 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00395a019
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  • 2
    Electronic Resource
    Electronic Resource
    THE EFFECTS OF AN ANTISERUM TO Na+, K+-ATPase ON THE ION-TRANSPORTING AND HYDROLYTIC ACTIVITIES OF THE ENZYME (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 242 (1974), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1974.tb19103.x
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  • 3
    Electronic Resource
    Electronic Resource
    (Na+K)-ATPase activity in cattle red cells (1974)
    [s.l.] : Nature Publishing Group
    Nature 249 (1974), S. 864-864 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR,-Schatzmann1 has described a positive correlation between ouabain-sensitive ATPase activity and red cell K levels in cattle, cells with higher K levels giving a greater enzyme activity. These determinations were made with Na=150 mM, K=10mM. If ouabain-sensitive ATPase is determined as a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/249864a0
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  • 4
    Electronic Resource
    Electronic Resource
    Net Synthesis of ATP by Reversal of the Sodium Pump (1970)
    [s.l.] : Nature Publishing Group
    Nature 225 (1970), S. 865-866 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The results of three experiments are summarized in Table 1. In each experiment, washed, pooled, guinea-pig red cells were pre-incubated in a nominally glucose-free high-K+ medium for 2 h or more. During at least part of this period iodoacetamide (5 mM) was present. In the first two experiments, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/225865a0
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  • 5
    Electronic Resource
    Electronic Resource
    The binding of cardiac glycosides to bull spermatozoa (1970)
    Springer
    Cellular and molecular life sciences 26 (1970), S. 20-21 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Resumen Se ha investigado la unión de glicósidos cardiacos al espermatozoide de toro. Dicha unión es sensible a inhibidores metabólicos y fué localizada en la membrana celular del segmento intermediario y la cola.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01900364
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  • 6
    Electronic Resource
    Electronic Resource
    Effects of high hydrostatic pressure on ‘passive’ monovalent cation transport in human red cells (1986)
    Springer
    The journal of membrane biology 94 (1986), S. 1-17 
    Details
    ISSN: 1432-1424
    Keywords: human red cell ; hydrostatic pressure ; ‘passive’ cation transport ; volume-sensitive KCl transport ; activation volume ; erythrocyte morphology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effects of high hydrostatic pressure (up to 400 ATA) on the ‘passive’ (defined as ouabain + bumetanide + EGTA-insensitive) influx and efflux of radiotracer cations (K+ Rb+, Na+, Cs+) has been studied in human red cells suspended at different medium tonicities giving altered cell volumes. Under all conditions studied, cation permeability was raised at pressure, and at least two distinct components were found to comprise this flux. Thus, increasing pressure (1) caused a generalized increase in cation permeability which was unaffected by the anion present, demonstrated linear concentration dependence, and wasreduced with cell swelling, and (2) stimulated a specific KCl pathway which was Cl− dependent, demonstrated saturation kinetics with raised [K]o and wasincreased with cell swelling. High hydrostatic pressure caused a significant alteration to red cell morphology from the normal biconcave disc to cup-shaped forms and it is proposed that this is associated with the unmasking of the volume-sensitive KCl system (2).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01901009
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  • 7
    Electronic Resource
    Electronic Resource
    Measurement and stoichiometry of bumetanide-sensitive (2Na∶1K∶3Cl) cotransport in ferret red cells (1985)
    Springer
    The journal of membrane biology 85 (1985), S. 205-213 
    Details
    ISSN: 1432-1424
    Keywords: sodium-potassium chloride cotransport ; red blood cells ; bumetanide ; stoichiometry ; ferret
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The bumetanide-sensitive uptake of Na+, K−(Rb−) and Cl− has been measured at 21°C in ferrent red cells treated with (SITS+DIDS) to minimize anion flux via capnophorin (Band 3). During the time course of the influx experiments tracer uptake was a first-order rate process. At normal levels of external Na+ (150mm) the bumetanide-sensitive uptake of K+ was dependent on Cl− and represented almost all of the K+ uptake, the residual flux demonstrating linear concentration dependence. The uptake of Na+ and Cl− was only partially inhibited by bumetanide indicating that pathways other than (Na+K+Cl) cotransport participate in these fluxes. The diuretic-sensitive uptake of Na+ or Cl− was, however, abolished by the removal of K+ or the complementary ion indicating that bumetanide-sensitive fluxes of Na+, K+ and Cl− are closely coupled. At very low levels of [Na] o (〈5mm) K+ influx demonstrated complex kinetics, and there was evidence of the unmasking of a bumetanide-sensitive Na+-independent K+ transport pathway. The stoichiometry of bumetanide-sensitive tracer uptake was 2Na∶1K∶3Cl both in cells suspended in a low and a high K+-containing medium. The bumetanide-sensitive flux was markedly reduced by ATP depletion. We conclude that a bumetanide-sensitive cotransport of (2Na∶1K∶3Cl) occurs as an electroneutral complex across the ferret red cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871515
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