The effect of low ATP concentrations on relaxation in the myosin regulated myofibrils from scallop |
| |
Authors: | Mary K. Knox Andrew G. Szent-Györgyi Cynthia E. Trueblood Annemarie Weber Sally Zigmond |
| |
Affiliation: | (1) Department of Biochemistry and Biophysics, University of Pennsylvania, 19104 Philadelphia, Pennsylvania, USA;(2) Department of Biology, Brandeis University, 02154 Waltham, Massachusetts, USA;(3) Department of Biology, University of Pennsylvania, 19104 Philadelphia, Pennsylvania, USA |
| |
Abstract: | Summary Troponin-tropomyosin-regulated myofibrils show a significant increase in ATPase activity and contract in the absence of calcium when the ATP concentration falls significantly below the saturation level. By contrast, the ATPase of the myosin-regulated myofibrils of scallop striated muscle was not activated in the absence of calcium when the ATP concentration was lowered to 10 mm. Nevertheless, a very small fraction of crossbridges were active at 10 mm ATP resulting in very slow myofibrillar shortening. In contrast to the behaviour of rabbit contractile proteins there was no correlation between myofibrillar shortening and ATP induced turbidity changes of actomyosin taken from scallop. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|