Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.
Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.
复制标题
caldesmon 抑制平滑肌肌动蛋白激活的肌球蛋白 Mg2 -ATP 酶活性。
DOI：
10.1016/s0021-9258(18)89793-9
复制
发表时间：
1984
期刊：
影响因子：
--
通讯作者：
M. Walsh
中科院分区：
文献类型：
--
作者：
P. Ngai;M. Walsh
Caldesmon是一种主要的钙调蛋白和肌动蛋白结合蛋白(Sobue，K.，Muramoto，Y.，Fujita，M.和Kakiuchi，S.(1981)proc.娜塔莉。阿卡德。SCI。美国A.78,5652-5655)，通过修改以前发表的程序(Ngai，P.K.，Carruthers，C.A.和Walsh，M.P.(1984)Biochem)，以高纯度的形式从鸡胆中获得。J.218,863-870)，并发现在由纯化的收缩蛋白和调节蛋白重组的系统中，超沉淀和肌动蛋白激活的肌球蛋白镁-ATPase活性均受到显著抑制，而不影响肌球蛋白的磷酸化状态。这种抑制作用在原肌球蛋白存在和不存在的情况下都可以看到。在鸡胆中发现了一种钙离子和钙调蛋白依赖的激酶，它催化钙调蛋白的磷酸化，与肌球蛋白轻链激酶不同。用钙调素-琼脂糖亲和层析法制备的钙调蛋白被钙蛋白激酶活性污染，不能抑制肌动球蛋白ATPase活性或超沉淀。在平滑肌中也发现了能够使钙调蛋白去磷酸化的磷酸酶活性。这些结果表明，Caldesmon在体外可以抑制平滑肌肌动球蛋白ATPase的活性，这种作用本身可能受到caldesmon可逆的磷酸化的调节。
Caldesmon, a major calmodulin- and actin-binding protein of smooth muscle (Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 5652-5655), has been obtained in highly purified form from chicken gizzard by a modification of a previously published procedure (Ngai, P. K., Carruthers, C. A., and Walsh, M. P. (1984) Biochem. J. 218, 863-870) and was found to cause a significant inhibition of both superprecipitation and actin-activated myosin Mg2+-ATPase activity in a system reconstituted from the purified contractile and regulatory proteins without influencing the phosphorylation state of myosin. This inhibitory effect was seen both in the presence and absence of tropomyosin. A Ca2+-and calmodulin-dependent kinase which catalyzed phosphorylation of caldesmon was identified in chicken gizzard; this kinase is distinct from myosin light-chain kinase. Caldesmon prepared by calmodulin-Sepharose affinity chromatography was contaminated with caldesmon kinase activity and was unable to inhibit actomyosin ATPase activity or superprecipitation. Phosphatase activity capable of dephosphorylating caldesmon was also identified in smooth muscle. These results indicate that caldesmon can inhibit smooth muscle actomyosin ATPase activity in vitro, and this function may itself be subject to regulation by reversible phosphorylation of caldesmon.
从心肌中纯化肌动蛋白。
DOI：
10.1080/00327488108065530
发表时间：
1981
期刊：
Preparative biochemistry
影响因子：
--
作者：
Zot,HG;Potter,JD
通讯作者：
Potter,JD