Praĭss R, Busse E, Banashak K H
Biokhimiia. 1978 Jan;43(1):58-66.
We could show an ATPase in mitochondrial and microsomal fractions of sheep arteria carotis communis and arteria coronaria of cattle which can be stimulated by Ca2+ of Mg2+, respectively. The enzyme has a higher affinity for Ca2+ than for Mg2+. The maximum activity of the Mg(Ca)-ATPase was found at 2-4 mM Ca2+ or Mg2+, respectively. Higher concentrations of these ions inhibit the enzyme. Mn2+, Sr2+ and Co2+ can substitute Ca2+ in splitting of ATP by the ATPase of both fractions of ateria coronaria of cattle. The ions K+ and Na+, variation of temperature and pH and a variety of pharmacological active compounds has the same effect on the ATPase stimulated by Ca2+ or Mg2+. These findings prove that Ca2+ and Mg2+ act at the same site of the ATPase of the mitochondrial and microsomal fraction of vascular smooth muscle.
我们能够在绵羊颈总动脉以及牛冠状动脉的线粒体和微粒体组分中展示出一种ATP酶,该酶分别可被Mg²⁺和Ca²⁺激活。这种酶对Ca²⁺的亲和力高于对Mg²⁺的亲和力。Mg(Ca)-ATP酶的最大活性分别在2-4 mM Ca²⁺或Mg²⁺时被发现。这些离子的较高浓度会抑制该酶。Mn²⁺、Sr²⁺和Co²⁺在牛冠状动脉两个组分的ATP酶分解ATP过程中可替代Ca²⁺。离子K⁺和Na⁺、温度和pH的变化以及多种药理活性化合物对由Ca²⁺或Mg²⁺激活的ATP酶具有相同的作用。这些发现证明Ca²⁺和Mg²⁺作用于血管平滑肌线粒体和微粒体组分ATP酶的同一部位。