Bottinelli R, Reggiani C
Institute of Human Physiology, University of Pavia, Italy.
Pflugers Arch. 1995 Feb;429(4):592-4. doi: 10.1007/BF00704166.
Force-velocity relations, myosin heavy chain (MHC) and myosin light chain (MLC) isoform composition of single skinned fibres from rat plantaris muscle were determined. In fibres containing the same (2X) isoform of myosin heavy chain, several parameters derived from the force-velocity relation and isometric force (Po) were tested for relation with the fibre content in alkali myosin light chain (MLC) isoforms. Whereas maximum shortening velocity was found to be proportional to the relative content in the 3f isoform of alkali MLC, velocity of shortening at 5% relative load, maximum power output, and Po were not. These results strengthen the idea that, in mammalian skeletal fibres, alkali MLC isoforms modulate shortening velocity at zero load, but suggest that they do not control the contractile behaviour at loads higher than zero.
测定了大鼠比目鱼肌单根去表皮纤维的力-速度关系、肌球蛋白重链(MHC)和肌球蛋白轻链(MLC)同工型组成。在含有相同(2X)肌球蛋白重链同工型的纤维中,测试了从力-速度关系和等长力(Po)得出的几个参数与碱性肌球蛋白轻链(MLC)同工型纤维含量的关系。虽然发现最大缩短速度与碱性MLC的3f同工型的相对含量成正比,但在5%相对负荷下的缩短速度、最大功率输出和Po并非如此。这些结果强化了这样一种观点,即在哺乳动物骨骼肌纤维中,碱性MLC同工型调节零负荷下的缩短速度,但表明它们不控制高于零负荷时的收缩行为。