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  • Contractility, 45-Ca Exchange  (1)
  • Flux Inhibition  (1)
  • Hemoglobin  (1)
  • Human immunodeficiency virus, seroprevalence, drug abuse, homosexuality,  (1)
Material
Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Psychiatry Research 39 (1991), S. 109-114 
    ISSN: 0165-1781
    Keywords: Human immunodeficiency virus, seroprevalence, drug abuse, homosexuality,
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Skeletal Muscle ; Electrolytes ; Potassium ; Sodium ; Flux Inhibition ; Membrane Stabilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2013
    Keywords: Myocardium ; Calcium-Magnesium Antagonism ; Contractility, 45-Ca Exchange
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4943
    Keywords: Hemoglobin ; recombinant hemoglobin ; protein folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
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