Polymerization of myosin from smooth muscle of the calf aorta.
Polymerization of myosin from smooth muscle of the calf aorta.
复制标题
来自小腿主动脉平滑肌的肌球蛋白聚合。
DOI：
10.1021/bi00511a006
复制
发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Lowey,S
中科院分区：
文献类型：
--
作者：
Megerman,J;Lowey,S
Joseph Megerman* and Susan Lowey* abstract: Myosin from smoothmuscle of the calf aorta has been found to be similar to rabbit skeletal muscle myosin in molecular weight, sedimentation coefficient, and amino acid composition. When dialyzed at low ionic strength, it also forms polymers that exist in equilibriumwith the “monomer”, the position of this equilibrium being sensitive to ionic strength, pH, and hydrostatic pressure. The self-association reactions for smooth muscle myosin differ, however, from those observed for skeletal muscle myosin in several ways:(1) aorta myosin polymerizes at a higher ionic strength to form a smaller polymer;(2) between pH 6 and 8, only one polymer boundary is observed;(3) the result of varying total protein concentration on the myosin-polymerequilibrium cannot be analyzed by the Gilbert theory for a simple two-species system, as was possible with skeletal myosin. This more complex polymerization behavior may be related to differences in the mode of assembly between smooth and skeletal muscle myosin. e contractile process in striated and vertebrate smooth muscles is thought to similarly depend on the interaction of thick and thin filaments (Needham, 1971). But the structure of the thick filamentsin the two types of muscle may be significantly different, even though myosin is the dominant component in both. In skeletal muscle, a bipolar structure results from myosin molecules oriented in opposite directions from either end of a central bare zone (Huxley, 1969). The structure of myosin filaments in vertebrate smooth muscles is less well-known because of their greater lability, and the reduced order of the filament matrix, which for many years delayed their visualization byelectron microscopy and X-ray diffraction [for a review, see Somlyo et al.(1977)]. Two basic configurations have been proposed: thebipolar structure described for striated muscle thick filaments (Ashton et al., 1975), and a “face-polar” structure that lacks a central bare zone, but has a single and opposite orientation of myosin cross bridges along the entire length of two sides of the filament (Small & Squire, 1972).
登录
查看更多内容
DOI：
10.1073/pnas.74.1.129
发表时间：
1977-01-01
影响因子：
11.1
作者：
CHACKO, S;CONTI, MA;ADELSTEIN, RS
通讯作者：
ADELSTEIN, RS
Machina Carnis：脊椎动物平滑肌
DOI：
--
发表时间：
1971
期刊：
影响因子：
--
作者：
D. Needham
通讯作者：
D. Needham
兔骨骼肌肌原纤维中肌钙蛋白、原肌球蛋白、肌动蛋白和肌球蛋白的含量。
影响因子：
3.9
作者：
J. Potter
通讯作者：
J. Potter
影响因子：
5.6
作者：
SMALL, JV;SQUIRE, JM
通讯作者：
SQUIRE, JM
子宫肌球蛋白的纯化和合成丝的形成。
影响因子：
5.6
作者：
P. Wachsberger;F. Pepe
通讯作者：
F. Pepe