Wuytack F, Raeymaekers L, Casteels R
Experientia. 1985 Jul 15;41(7):900-5. doi: 10.1007/BF01970008.
A calmodulin stimulated Ca2+-transport ATPase which has many of the characteristics of the erythrocyte type Ca2+-transport ATPase has been purified from smooth muscle. In particular, the effect of calmodulin on these transport enzymes is mimicked by partial proteolysis and antibodies against erythrocyte Ca2+-transport ATPase also bind to the smooth muscle (Ca2+ + Mg2+)ATPase. A correlation between the distribution of the calmodulin stimulated (Ca2+ + Mg2+)ATPase and (Na+ + K+)ATPase activities in smooth muscle membranes separated by density gradient centrifugation suggests a plasmalemmal distribution of this (Ca2+ + Mg2+)ATPase. A phosphoprotein intermediate in smooth muscle which strongly resembles the corresponding phosphoprotein in sarcoplasmic reticulum of skeletal muscle may indicate the presence in smooth muscle of a similar type of Ca2+-transport ATPase.
一种受钙调蛋白刺激的Ca2+转运ATP酶已从平滑肌中纯化出来,它具有许多红细胞型Ca2+转运ATP酶的特征。特别是,钙调蛋白对这些转运酶的作用可被部分蛋白水解模拟,并且抗红细胞Ca2+转运ATP酶的抗体也能与平滑肌(Ca2+ + Mg2+)ATP酶结合。通过密度梯度离心分离的平滑肌膜中,钙调蛋白刺激的(Ca2+ + Mg2+)ATP酶活性与(Na+ + K+)ATP酶活性的分布之间的相关性表明,这种(Ca2+ + Mg2+)ATP酶分布于质膜。平滑肌中的一种磷蛋白中间体与骨骼肌肌浆网中的相应磷蛋白非常相似,这可能表明平滑肌中存在类似类型的Ca2+转运ATP酶。