Cross-linking within the thick filaments of muscle and its effect on contractile force.
Cross-linking within the thick filaments of muscle and its effect on contractile force.
复制标题
肌肉粗丝内的交联及其对收缩力的影响。
DOI：
10.1021/bi00386a051
复制
发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Harrington,WF
中科院分区：
文献类型：
--
作者：
Ueno,H;Harrington,WF
约翰霍普金斯大学麦科勒姆-普拉特研究所生物系，马里兰州巴尔的摩21218摘要：我们研究了交联对甘油化腰肌纤维的跨桥运动和等距力的影响。采用两种不同的方法，高孔隙率凝胶电泳和分离技术，跟踪肌球蛋白头（亚片段1）和棒段与粗丝主干的交联。与早期报道相反[Sutoh， K., & Harrington， W. F.(1977) Biochemistry 16, 2441-2449；Sutoh， K., Chiao， Y. C., & Harrington， W. F.（1978）生物化学17,1234-1239；Chiao， Y. C, & Harrington， W. F.(1979) Biochemistry（生物化学）18959 -963)，我们发现肌球蛋白分子的头部并没有通过亚亚酰二甲基与粗丝表面交联。在核心内的交联棒段的时间依赖性是通过二硫氧化程序来监测的，以区分分子间和分子内的交联。将肌原纤维内交联反应的程度与交联不同阶段纤维内产生的等距力进行比较，发现等距力随着高分子量（交联）棒材的形成而消失（> A/r 1000K）。肌纤维atp酶几乎不受交联反应的影响。
Department of Biology, McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218 Received October 20, 1986; Revised Manuscript Received February 18, 1987 abstract: We have examined the effect of cross-linking on cross-bridge movement and isometric force in glycerinated psoas fibers. Two different methods, high-porosity gel electrophoresis and a fractionation technique, were used to follow the cross-linking of myosin heads (subfragment 1) and rod segments to the thick filament backbone. Contrary to earlierreports [Sutoh, K., & Harrington, W. F.(1977) Biochemistry 16, 2441-2449; Sutoh, K., Chiao, Y. C., & Harrington, W. F.(1978) Biochemistry 17, 1234-1239; Chiao, Y. C., & Harrington, W. F.(1979) Biochemistry 18,959-963], we find that the heads of the myosin molecules are not cross-linked to the thick filament surface by dimethyl suberimidate. The time dependence of cross-linking rod segments within the core was monitored by a disulfide oxidation procedureto distinguish between intermolecular and intramolecular cross-linking. Comparison of theextent of the cross-linking reaction within myofibrils and the isometric force developed within fibers at various stages of cross-linking shows that isometric force is abolished in parallel with the formation of high molecular weight (cross-linked) rod species (> A/r 1000K). The myofibrillar ATPase remains virtually unaffected by the cross-linking reaction.