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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 350 (1974), S. 321-334 
    ISSN: 1432-2013
    Keywords: Skeletal Muscle ; Contractility ; Magnesium ; Calcium ; Excitation-Contraction ; Coupling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The penetration of magnesium from high-Mg Ringer's solution into skeletal muscle, and accompanying effects on intrafibre electrolyte composition, muscle contractility and Ca-exchange have been studied in isolated preparations of whole sartorius ofRana temporaria. Muscle magnesium, corrected for extracellular space, rose rapidly and then more slowly, and at 60 min in 20 mM Mg-Ringer it was calculated that intrafibre unbound Mg was increased by at least two-fold over the level in companion muscles in normal Ringer. Contractile response to direct, supramaximal stimulation was reduced in Mg-loaded muscles while resting membrane potential (E m) remained unaffected. Contracture in response to high-K was diminished while caffeine contracture was not changed. Muscles loaded with Mg also showed significant loss of fibre K and gained Na. Mg-loading caused a significant decrease in exchangeability of muscle Ca. Three fractions of exchangeable Ca in muscle were detected, characterised by half-times of circa 1.5, 7 and 50 min, respectively. In muscles soaked in high-Mg Ringer the half-times for these fractions were not different to the controls, but the quantities exchanged in the two slower fractions were reduced.
    Type of Medium: Electronic Resource
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  • 2
    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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