Comparison of the fluorescence and conformational properties of smooth and striated tropomyosin.
Comparison of the fluorescence and conformational properties of smooth and striated tropomyosin.
复制标题
平滑和条纹原肌球蛋白的荧光和构象特性的比较。
DOI：
10.1021/bi00303a001
复制
发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Seidel,JC
中科院分区：
文献类型：
--
作者：
Lehrer,SS;Betteridge,DR;Graceffa,P;Wong,S;Seidel,JC
舍温Lehrer，** 大卫R. Betteridge，Philip Graceffa，Sunny Wong，and John C.赛德尔摘要：与以往对兔骨骼肌和心肌原肌球蛋白的构象研究相反，（i）当鸡砂囊原肌球蛋白的半胱氨酸侧链与5，5 ′-二硫代双（2-硝基苯甲酸酯）时，不产生链间二硫键交联，（ii）当它们用芘基马来酰亚胺标记时，未观察到受激准分子荧光，和（iii）当它们用双丹酰胱氨酸标记时，长寿命的荧光成分在包括原肌球蛋白在内的大温度范围内对荧光衰减没有明显的贡献。原肌球蛋白是横纹肌和平滑肌细丝的成分（Small和Sobieszek，1983）。在横纹肌系统中，其与肌钙蛋白一起参与收缩的Ca 2+依赖性细丝调节（Ebashi & Endo，1968），而其在平滑肌中的作用不太清楚，因为调节似乎是通过粗细丝上肌球蛋白的Ca 2+依赖性磷酸化来完成的（Chacko et al.，1977; Gorecka等人，1976; Sobieszek & Small，1976）。
Sherwin S. Lehrer,** David R. Betteridge, Philip Graceffa, Sunny Wong, and John C. Seidel abstract: In contrast toprevious conformational studies with rabbit skeletal and cardiac tropomyosins,(i) when the cysteine side chains of chicken gizzard tropomyosin were reacted with 5, 5'-dithiobis (2-nitrobenzoate), an interchain disulfide cross-link was not produced,(ii) when they were labeled with py-renylmaleimide, excimer fluorescence was not observed, and (iii) when they were labeled with didansylcystine, a long-lived fluorescence component did not appreciably contribute to the fluorescence decay over a large temperature range includingTropomyosin is a component of striated and smooth muscle thin filaments (Small & Sobieszek, 1983). In striated muscle systems, in conjunction with troponin, it is involved in the Ca2+-dependent thin filament regulation of contraction (Ebashi & Endo, 1968), whereas its role in smooth muscle is less clear since regulation appears to be accomplished via a Ca2+-dependent phosphorylation of myosin on the thick filament (Chacko et al., 1977; Gorecka et al., 1976; Sobieszek & Small, 1976).