The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments.
The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments.
复制标题
caldesmon 对骨骼肌肌动球蛋白 ATP 酶活性和肌动蛋白丝成束的影响。
DOI：
10.1016/0304-4165(85)90295-8
复制
发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Hanna Osińska
中科院分区：
文献类型：
--
作者：
R. Da̧browska;Andrzej Goch;B. Gała̧zkiewicz;Hanna Osińska
鸡砂囊钙调蛋白对兔骨骼肌肌动球蛋白Mg ~（2+）-ATP酶活性的抑制达40%。在存在的鸡砂囊原肌球蛋白这种抑制显着增加，达到最大值（约80%），在1至10-13的钙调蛋白肌动蛋白单体的摩尔比。肌动球蛋白ATP酶的抑制发生在较宽的pH范围内（从6.0到8.0），但随着KCl和MgCl_2浓度的增加而减少。钙调素在其抑制肌动球蛋白ATP酶的钙调素/肌动蛋白比率范围内，形成成束的平行排列的肌动蛋白丝。钙调素在Ca 2+存在下解离这些束并抑制肌动球蛋白ATP酶的抑制，条件是它以高摩尔过量使用。
Chicken gizzard caldesmon causes up to 40% inhibition of Mg2+-ATPase activity of rabbit skeletal muscle actomyosin. In the presence of chicken gizzard tropomyosin this inhibition is significantly increased, reaching a maximum (around 80%) at a molar ratio of caldesmon to actin monomer of 1 to 10–13. The inhibition of actomyosin ATPase takes place over a wide pH range (from 6.0 to 8.0) but is decreased with an increase in KCl and MgCl2concentrations. Caldesmon, in the range of caldesmon/actin ratios within which it inhibits actomyosin ATPase, forms bundles of parallelly aligned actin filaments. Calmodulin in the presence of Ca2+dissociates these bundles and restrains the inhibition of actomyosin ATPase, provided that it is used at a high molar excess over caldesmon.