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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 27 (1988), S. 5885-5890 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    ISSN: 1573-6881
    Keywords: (Ca2+ + Mg2+)-ATPase ; sarcoplasmic reticulum ; membrane fluidity ; enzyme kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum has been reconstituted with dipalmitoylphosphatidylcholine, and the activating effect of ATP and Ca2+ on this enzyme has been studied at different temperatures. It has been found that two kinetic forms of the enzyme are interconverted at about 31°C, and this is possibly related to a phase change in the phospholipid which is more directly associated with the protein. Above 31°C the enzyme is less dependent on ATP activation at high ATP concentrations but shows positive cooperativity for Ca2+ activation. On the other hand, below 31°C, the reconstituted enzyme is more dependent on ATP for activation at high ATP concentrations than the purified ATPase and does not show cooperativity for Ca2+ activation.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    ISSN: 1573-6881
    Keywords: (Ca2+-Mg2+)-ATPase ; sarcoplasmic reticulum ; enzyme kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The (Ca2+-Mg2+)-ATPase from sarcoplasmic reticulum presents negative cooperativity for the hydrolysis of Mg2+-ATP at different concentration ranges of this substrate. A kinetic model is proposed according to which Mg2+-ATP may bind to three different enzymatic species present during the catalytic cycle, E (K 1=1 µM), E′∼P.Ca2 (K 9=500 µM) and *EP (K 7=20 µM), accelerating the release of Pi. The fact that each of these species has a different affinity for Mg2+-ATP allows a significant enhancement of the rate of Pi release to the medium at the different ranges of Mg2+-ATP concentration where the enzyme shows a kinetic cooperativity. The kinetic analysis of this mechanism yields an equation which is a ratio of two cubic polynomials (3:3 rate equations) with respect to Mg2+-ATP and which may explain the negative cooperativity of the enzyme at different concentration ranges of Mg2+-ATP.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 8247-8254 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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