大鼠肝脏微粒体部分钙离子刺激的ATP酶的一些特性。
Some properties of the Ca2+-stimulated ATPase of a rat liver microsomal fraction.
作者信息
Dawson A P, Fulton D V
出版信息
Biochem J. 1983 Feb 15;210(2):405-10. doi: 10.1042/bj2100405.
Abstract
- The heavy microsomal fraction from rat liver apparently has very little Ca2+-stimulated ATPase activity, although it has an active, ATP-driven Ca2+ accumulation system. 2. The addition of ionophore A23187 to the ATPase assay, to allow continuous Ca2+ recycling during the assay time, reveals the presence of a substantial Ca2+-stimulated ATPase with Vmax. 160 nmol of Pi/10 min per mg of protein and Km for Ca2+ 0.19 microM. 3. The Ca2+-stimulated ATPase, but not the basal Mg2+-stimulated ATPase, is potently inhibited by orthovanadate. Both the Ca2+-stimulated ATPase and the vanadate inhibition are enhanced by the presence of Mg2+. 4. Ca2+-stimulated ATPase activity is not responsive to calmodulin or the calmodulin antagonist trifluoperazine.
摘要
- 大鼠肝脏的重微粒体部分显然几乎没有Ca2+刺激的ATP酶活性，尽管它有一个活跃的、由ATP驱动的Ca2+积累系统。2. 在ATP酶测定中加入离子载体A23187，以便在测定期间实现Ca2+的持续循环，结果显示存在一种大量的Ca2+刺激的ATP酶，其Vmax为每毫克蛋白质每分钟160 nmol无机磷，Ca2+的Km为0.19 microM。3. Ca2+刺激的ATP酶，而不是基础的Mg2+刺激的ATP酶，受到原钒酸盐的强烈抑制。Mg2+的存在会增强Ca2+刺激的ATP酶活性和钒酸盐抑制作用。4. Ca2+刺激的ATP酶活性对钙调蛋白或钙调蛋白拮抗剂三氟拉嗪没有反应。
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