Blyakhman F A, Shklyar T, Pollack G H
Department of Bioengineering, University of Washington, Seattle 98195, USA.
J Muscle Res Cell Motil. 1999 Aug;20(5-6):529-38. doi: 10.1023/a:1005590401721.
The time course of shortening was investigated in the single sarcomere, the smallest contractile unit that retains natural structure. We projected the striation patterns of single bumblebee flight-muscle myofibrils onto a linear photodiode array, which was scanned periodically to produce repetitive traces of intensity vs. position along the array. Sarcomere length was taken as the span between adjacent A-band or Z-line centroids. When myofibrils were ramp-released by a motor, individual sarcomeres shortened in steps punctuated by pauses. The single sarcomere-shortening trace was consistently stepwise both in activated and relaxed specimens. Although step size was variable, the size distribution showed a signature-like feature: the histogram comprised distinct peaks that were spaced quasi-regularly. In the activated myofibrils the interpeak separation corresponded to 2.71 nm per half-sarcomere. This value is equal to the linear advance of actin subunits along the thin filament. Thus, actin filaments translate over thick filaments by steps that may be integer multiples of the actin-subunit spacing.
我们研究了单个肌节(保留自然结构的最小收缩单位)缩短的时间进程。我们将单个大黄蜂飞行肌肌原纤维的条纹模式投射到线性光电二极管阵列上,该阵列会定期扫描,以生成沿阵列强度与位置的重复轨迹。肌节长度被视为相邻A带或Z线质心之间的跨度。当通过电机对肌原纤维进行斜坡释放时,单个肌节会以停顿为间隔逐步缩短。在激活和松弛的标本中,单个肌节缩短轨迹始终呈阶梯状。尽管步长可变,但大小分布呈现出类似特征:直方图由间隔近似规则的不同峰值组成。在激活的肌原纤维中,峰间间距相当于每个半肌节2.71纳米。这个值等于肌动蛋白亚基沿细肌丝的线性推进距离。因此,肌动蛋白丝沿粗肌丝平移的步长可能是肌动蛋白亚基间距的整数倍。