Intramolecular Oscillation of the Phosphorylation Domain of Rat Cardiac Sarcoplasmic Reticulum Titrated with Arachidonoyl Phosphatidylcholine.

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概要

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• Sarcoplasmic reticulum vesicles were prepared from rat myocardium. The intramolecular oscillation of the phosphorylation domain of Ca2+-ATPase in control vesicles and in vesicles titrated with diarachidonoyl phosphatidylcholine was studied with a nanosecond time-resolved fluorometer. The membrane viscosity of the lipid domain was decreased by the lipid titration. The phosphorylation domain was labeled with a fluorophore, anilinonaphthylmaleimide (ANM). The time course of anisotropy decay of ANM fluorescence reflects the localized oscillation in the protein structure. The half-decay time of the anisotropy was decreased by diarachidonoyl titration from 77 nsec in control vesicles to 66 nsec, suggesting an increase in the intramolecular oscillation. Concomitantly observed decreases in membrane viscosity and Ca2+-ATPase activity suggest that the decreased membrane viscosity destabilized the Ca2+-ATPase protein structure causing a reduction in Ca2+-ATPase activity.

• International Heart Journal刊行会の論文

著者

• KOYAMA Tomiyasu

  Section of Physiology, Research Institute of Applied Electricity, Hokkaido University

• ZHU Ming-Yan

  Section of Physiology, Research Institute of Applied Electricity, Hokkaido University

関連論文

• Intramolecular Oscillation of the Phosphorylation Domain of Rat Cardiac Sarcoplasmic Reticulum Titrated with Arachidonoyl Phosphatidylcholine.
• Dynamic microstructure of mitochondrial membranes from rabbit heart subjected to reperfusion after ischemia.

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