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.
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Teruel, J.A., Delicado, E.G., Villalaín, J. et al. Modulation of the kinetic characteristics of the sarcoplasmic reticulum ATPase by membrane fluidity. J Bioenerg Biomembr 18, 113–122 (1986). https://doi.org/10.1007/BF00743480
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DOI: https://doi.org/10.1007/BF00743480