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  • Contractility, 45-Ca Exchange  (1)
  • Flux Inhibition  (1)
  • Hemoglobin  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Influence of the membrane stabilizer diphenylhydantion on potassium and sodium movements in skeletal muscle (1975)
    Springer
    Pflügers Archiv 358 (1975), S. 275-288 
    Details
    ISSN: 1432-2013
    Schlagwort(e): Skeletal Muscle ; Electrolytes ; Potassium ; Sodium ; Flux Inhibition ; Membrane Stabilization
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The membrane stabilizer diphenylhydantoin (DPH) did not alter the net content of Na, K, Ca or Mg in frog sartorius muscle freshly incubated or actively transporting Na and K following Na-loading and K-depletion. Resting influx of K from normal Ringer was significantly reduced by DPH, and this inhibition occurred in the ouabain-insensitive K-uptake. Inhibition of K-influx by DPH was overcome when [K]0 was raised to 10 mM, and Rb-influx was not sensitive to the inhibitor in 2.5 mM Rb-Ringer. Efflux of tracer K was reduced by DPH in the presence and absence of ouabain. Exchange of muscle Na was not affected under condit in which K-exchange was significantly reduced, but DPH appeared to cause increased net loss of Na from muscles washed in Na-free medium. The inhibition by DPH of resting K-exchange was not sensitive to wide variations in [Na]0 or in [Ca]0. The results suggest that the effect of DPH on frog skeletal muscle in normal ionic environment is to reduce the resting, passive component of K-exchange across the fibre membrane. This effect is discussed in relation to the membrane stabilizing actions of diphenylhydantoin.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00587224
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  • 2
    Digitale Medien
    Digitale Medien
    An analysis of calcium-magnesium antagonism in contractility and ionic balance in isolated trabecular muscle of rat ventricle (1975)
    Springer
    Pflügers Archiv 360 (1975), S. 267-282 
    Details
    ISSN: 1432-2013
    Schlagwort(e): Myocardium ; Calcium-Magnesium Antagonism ; Contractility, 45-Ca Exchange
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The influence of elevated Mg (20 mM) on mechanical response, fibre electrolyte composition and Ca-exchange, as a function of external Ca concentration, has been studied in an isolated trabecular muscle column of rat ventricle. At [Ca]0 2.5 mM, cellular Mg-content increased in 20 mM [Mg]0 without effect on contractility or fibre content of other electrolytes. As [Ca]0 was reduced from 2.5 mM, 20 mM Mg caused progressive inhibition of contractile response of muscle to electrical stimulation. In both resting and stimulated trabeculae the intrafibre Mg-content rapidly increased and Ca-content fell in the initial 20 min incubation in reduced (1.5 or 0.75 mM) Ca, as the contractile response declined. Subsequent restoration of [Ca]0 to 2.5 mM restored contractile response in the presence of high Mg concentration. Exposure of trabeculae to high Mg also caused a significant decrease in 45-Ca exchange in a muscle calcium-pool exchanging witht1/2 7 min when [Ca]0 was 1.5 mM, but had no effect on Ca-exchange when [Ca]0 was 2.5 mM. The effect of high Mg on exchange of Ca indicated that displacement of a fraction of superficially-bound muscle Ca was responsible for the diminished contractile response in Mg-loaded trabeculae.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00583721
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  • 3
    Digitale Medien
    Digitale Medien
    Recombinant human hemoglobin: Expression and refolding of β-globin fromEscherichia coli (1991)
    Springer
    The protein journal 10 (1991), S. 495-501 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Hemoglobin ; recombinant hemoglobin ; protein folding
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract A plasmid analogous to the one described by Nagai and Thogersen (Nature,309, 810–812, 1984) has been constructed for the expression of globins inE. coli. Induction with nalidixic acid produces high yields of a fusion protein, NS1-FX-β-globin, where NS1 represents 81 residues of a flu virus protein and FX represents a blood-clotting Factor Xa recognition sequence, Ile-Glu-Gly-Arg. This fusion protein is readily solubilized in 50 mM NaOH and remains in solution when thepH is adjusted to 8.6. Under these conditions, the fusion protein is hydrolyzed by activated Factor X, giving authentic β-globin which can be folded in the presence of cyanohemin and native α-chains to produce a tetrameric hemoglobin with the functional properties of natural human hemoglobin.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025477
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