Modulation of the actin-activated adenosinetriphosphatase activity of myosin by tropomyosin from vascular and gizzard smooth muscles.

Modulation of the actin-activated adenosinetriphosphatase activity of myosin by tropomyosin from vascular and gizzard smooth muscles.
复制标题

来自血管和砂囊平滑肌的原肌球蛋白对肌球蛋白的肌动蛋白激活的腺苷三磷酸酶活性的调节。

DOI:
10.1021/bi00299a029
复制
发表时间:
1984
期刊:
影响因子:
2.9
通讯作者:
Seidel,JC
Seidel,JC
中科院分区:
生物学3区
文献类型:
--
作者:
Yamaguchi,M;Ver,A;Carlos,A;Seidel,JC

文献摘要

被引文献

相似文献

Masahiro Yamaguchi,** Agota Ver,§Aida Carlos和John C. Seidel*摘要:牛主动脉和肺动脉原肌球蛋白在十二基硫酸钠中表现出相同的电泳模式,但与鸡沙棘或兔骨骼肌的原肌球蛋白不同。四种原肌球蛋白中的每一种都很容易与骨骼肌f -肌动蛋白结合,这表明它们与肌动蛋白的沉淀以及它们以每七个肌动蛋白单体一个原肌球蛋白的摩尔比最大限度地刺激或抑制肌动蛋白激活的atp酶活性的能力。平滑肌原肌球蛋白和骨骼肌原肌球蛋白对骨骼肌球蛋白或重肌球蛋白(HMM)活性的影响不同;前者可以在后者抑制的条件下增强活性。砂囊原肌球蛋白和动脉原肌球蛋白在刺激骨骼atp酶活性方面通常同样有效
Masahiro Yamaguchi,** Agota Ver, § Aida Carlos, and John C. Seidel* abstract: Tropomyosins from bovine aorta and pulmonary artery exhibit identical electrophoretic patterns in sodium dodecyl sulfate but differ from tropomyosins of either chicken gizzard or rabbit skeletal muscle. Each of the four tropo-myosins binds readily to skeletalmuscle F-actin as indicated by their sedimentation with actin and by their ability to maximally stimulate or inhibit actin-activated ATPase activity at a molar ratio of one tropomyosin per seven actin monomers. Smooth and skeletal muscle tropomyosins differ in their effects on activity of skeletal myosin or heavy meromyosin (HMM); the former can enhance activity under conditions in which the latter inhibits. Gizzard and arterial tropomyosins are usually equally effective in stimulating ATPase activityof skeletal