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Inactivation of Ca2+ uptake and ATPase activity of the Ca2(+)-ATPase of rabbit sarcoplasmic reticulum was measured and compared to the thermal denaturation of the enzyme as measured by differential scanning calorimetry (DSC) and fluorescence spectroscopy. Two fluorophores were monitored: intrinsic tryptophan (localized in the transmembrane region) and(More)
Differential scanning calorimetry (DSC) was used to assay thermal transitions that might be responsible for cell death and other responses to hyperthermia or heat shock, such as induction of heat shock proteins (HSP), in whole Chinese hamster lung V79 cells. Seven distinct peaks, six of which are irreversible, with transition temperatures from 49.5 degrees(More)
The thermodynamic parameters characterizing protein folding can be obtained directly using differential scanning calorimetry (DSC). They are meaningful only for reversible unfolding at equilibrium, which holds for small globular proteins; however, the unfolding or denaturation of most large, multidomain or multisubunit proteins is either partially or(More)
The site of interaction of dibucaine with the Ca(2+)-ATPase of rabbit sarcoplasmic reticulum, an ion-transporting membrane protein, was investigated by determining the effect of dibucaine on the denaturation of the transmembrane domain and the aqueous domain containing, respectively, the high-affinity Ca2+ binding sites and the site of ATP hydrolysis. In(More)
Left ventricle dimensions and wall stress were measured echocardiographically before and immediately after exercise in 14 athletes and 7 control subjects. Our findings suggest that afterload is an important determinant of cardiac performance and wall hypertrophy in athletes. In spite of major changes in heart rate and blood pressure, left ventricular wall(More)
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