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在等长和等张收缩过程中,对活蛙缝匠肌中肌球蛋白头部运动进行时间分辨X射线衍射研究。

Time-resolved X-ray diffraction studies of myosin head movements in live frog sartorius muscle during isometric and isotonic contractions.

作者信息

Martin-Fernandez M L, Bordas J, Diakun G, Harries J, Lowy J, Mant G R, Svensson A, Towns-Andrews E

机构信息

SERC Daresbury Laboratory, Warrington, UK.

出版信息

J Muscle Res Cell Motil. 1994 Jun;15(3):319-48. doi: 10.1007/BF00123484.

Abstract

Using the facilities at the Daresbury Synchrotron Radiation Source, meridional diffraction patterns of muscles at ca 8 degrees C were recorded with a time resolution of 2 or 4 ms. In isometric contractions tetanic peak tension (P0) is reached in ca 400 ms. Under such conditions, following stimulation from rest, the timing of changes in the major reflections (the 38.2 nm troponin reflection, and the 21.5 and 14.34/14.58 nm myosin reflections) can be explained in terms of four types of time courses: K1, K2, K3 and K4. The onset of K1 occurs immediately after stimulation, but that of K2, K3 and K4 is delayed by a latent period of ca 16 ms. Relative to the end of their own latent periods the half-times for K1, K2, K3 and K4 are 14-16, 16, 32 and 52 ms, respectively. In half-times, K1, K2, K3 lead tension rise by 52, 36 and 20 ms, respectively. K4 parallels the time course of tension rise. From an analysis of the data we conclude that K1 reflects thin filament activation which involves the troponin system; K2 arises from an order-disorder transition during which the register between the filaments is lost; K3 is due to the formation of an acto-myosin complex which (at P0) causes 70% or more of the heads to diffract with actin-based periodicities; and K4 is caused by a change in the axial orientation of the myosin heads (relative to thin filament axis) which is estimated to be from 65-70 degrees at rest to ca 90 degrees at P0. Isotonic contraction experiments showed that during shortening under a load of ca 0.27 P0, at least 85% of the heads (relative to those forming an acto-myosin complex at P0) diffract with actin-based periodicities, whilst their axial orientation does not change from that at rest. During shortening under a negligible load, at most 5-10% of the heads (relative to those forming an acto-myosin complex at P0) diffract with actin-based periodicities, and their axial orientation also remains the same as that at rest. This suggests that in isometric contractions the change in axial orientation is not the cause of active tension production, but rather the result of it. Analysis of the data reveals that independent of load, the extent of asynchronous axial motions executed by most of the cycling heads is no more than 0.5-0.65 nm greater than at rest.(ABSTRACT TRUNCATED AT 400 WORDS)

摘要

利用达雷斯伯里同步辐射源的设备,在约8摄氏度下记录肌肉的子午衍射图案,时间分辨率为2或4毫秒。在等长收缩中,强直收缩峰值张力(P0)在约400毫秒时达到。在这种条件下,从静止状态受到刺激后,主要反射(38.2纳米肌钙蛋白反射以及21.5和14.34/14.58纳米肌球蛋白反射)变化的时间进程可以用四种时间过程来解释:K1、K2、K3和K4。K1在刺激后立即开始,但K2、K3和K4的开始延迟约16毫秒的潜伏期。相对于它们各自潜伏期的结束,K1、K2、K3和K4的半衰期分别为14 - 16毫秒、16毫秒、32毫秒和52毫秒。在半衰期方面,K1、K2、K3分别比张力上升提前52毫秒、36毫秒和20毫秒。K4与张力上升的时间进程平行。通过对数据的分析,我们得出结论:K1反映涉及肌钙蛋白系统的细肌丝激活;K2源于细丝之间的对齐丢失的有序 - 无序转变;K3是由于肌动蛋白 - 肌球蛋白复合物的形成,该复合物(在P0时)导致70%或更多的头部以基于肌动蛋白的周期性衍射;K4是由肌球蛋白头部的轴向取向变化引起的(相对于细肌丝轴),估计从静止时的65 - 70度变为P0时的约90度。等张收缩实验表明,在约0.27P0的负荷下缩短过程中,至少85%的头部(相对于在P0时形成肌动蛋白 - 肌球蛋白复合物的头部)以基于肌动蛋白的周期性衍射,而它们的轴向取向与静止时相比没有变化。在可忽略负荷下缩短过程中,最多5 - 10%的头部(相对于在P0时形成肌动蛋白 - 肌球蛋白复合物的头部)以基于肌动蛋白的周期性衍射,并且它们的轴向取向也与静止时相同。这表明在等长收缩中,轴向取向的变化不是主动张力产生的原因,而是其结果。对数据的分析表明,与负荷无关,大多数循环头部执行的异步轴向运动程度比静止时不超过0.5 - 0.65纳米。(摘要截断于400字)

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