Calcium Binding and Enzymatic Activities of Cell Membrane Isolated from Cardiac Muscle
スポンサーリンク
概要
- 論文の詳細を見る
Cell membrane was isolated from porcine ventricles and its Ca<SUP>2+</SUP> binding and ATPase activities were investigated. The cell membrane (heart sarcolemma) exhibits Na<SUP>+</SUP>-K<SUP>+</SUP>activated ATPase and Ca<SUP>2+</SUP> stimulated. Mg-ATPase activities which suggest the presence of "Ca-pump"system.<BR>Ca<SUP>2+</SUP> binding to the cell membrane was dependent on Ca<SUP>2+</SUP> concentration and analysis of binding curve revealed that the existence of two kinds of binding sites (high and low affinity sites). Mg<SUP>2+</SUP> increased Ca<SUP>2+</SUP> binding at the high affinity site whereas Na<SUP>+</SUP> decreased it. These actions of Mg<SUP>2+</SUP> and Na<SUP>+</SUP> may be physiologically important for the maintenance and transient change of intracellular Ca<SUP>2+</SUP> concentration at rest and excitation of the membrane
- 日本膜学会の論文