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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 2 (1970), S. 1-16 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Measurements of interfacial electron flow indicate that membrane fragments rich in Na+−K+-ATPase are capable of absorbing and releasing electrons in the form of random currents at an electrode surface. The electron transporting system, which functions in the presence or absence of substrate and activating ions, may be part of or in contact with the enzyme system, but it is not related to the ATPase activity. The observed electron transport at an electrode surface resembles physiological electron transport processes in being reversible, in extending over the same range of potential, and in being affected by some of the chemicals that interfere with electron transport and oxidative phosphorylation in mitochondria. Our experiments do not provide sufficient evidence to identify the substances that are responsible for the random currents, but the results suggest that the electro-active substances are similar to those which are involved in the reactions at the second phosphorylation site in mitochondria. Experiments with this technique provide a new approach to the study of the mechanism of biological electron transport processes and their possible relation to ATP synthesis and hydrolysis.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 47 (1979), S. 185-193 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The pressure-area isotherm and shear resistance of spectrin-actin monolayers indicate a close-packed structure at about 1.0 m2/mg protein. This surface area is equivalent to a thickness of about two monolayers at the erythrocyte membrane inner face. The maximum elasticity (lowest compressibility) occurs at 0.7 m2/mg protein, indicating the limit of reversible compression. The mechanical properties of the monolayers approximate those of the intact membrane, suggesting that the structures are similar and that these monolayers may account for many of thein vivo properties.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 1 (1969), S. 238-247 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The action of phloridzin and simple sugars on the (Na+−K+)-activated ATPase obtained from rabbit kidney has been studied. Phloridzin 10−4to 10−3 m was found to inhibit the enzyme at Na+:K+ ratios less than optimal for enzyme activity, whereas stimulation was noted at Na+:K+ ratios greater than optimal for enzyme activity. Some sugars in concentrations of 0.1 to 0.5m were found to inhibit the (Na+−K+)-activated ATPase. The sugars and related compounds could be ranked according to decreasing inhibitory potency as: D-mannose〉D-arabinose, D-xylose〉L-xylose〉D-glucose〉fructose, L-arabinose〉D-galactose, myo-inositol, mannitol=0. No stimulatory effect or interaction with K+ was found with these compounds. The action of these substances on the (Na+−K+)-activated ATPase suggests an interaction of actively transported sugars and sodium-potassium transport at the level of the sodium pump that may be important in the biological coupling of the two systems.
    Type of Medium: Electronic Resource
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