Nonparallel isometric tension response of rabbit soleus skinned muscle fibers to magnesium adenosine triphosphate and magnesium inosine triphosphate.
Open Access
- 1 August 1979
- journal article
- research article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 74 (2) , 261-274
- https://doi.org/10.1085/jgp.74.2.261
Abstract
The isometric tension response of single skinned rabbit soleus muscle fibers to MgATP and MgITP in the absence of Ca was studied. [MgATP] or [MgITP] was varied in solutions of ionic strength 0.30 and temperature 20.degree. C. Steady-state tension that developed in MgATP or MgITP solutions was a biphasic bell-shaped function of log [MgATP] or log [MgITP] which increased from zero to maximum tension and then declined again to zero. Under comparable ionic conditions, percent tension vs. log [MgATP] and percent tension vs. log [MgITP] curves are not parallel. Instead, the percent tension vs. log [MgITP] curve is much broader. Under comparable ionic conditions maximum tension in MgITP solutions was higher than in MgATP solutions. In MgATP solutions, pH, [K+], and excess ATP were varied. Raising pH from 7 to 8, [K+] from 46 mM to 200 mM, or decreasing excess ATP from 2 to 0.5 mM all increased maximum tension. None of these factors influenced the shape or position of the percent tension vs. log [MgATP] curve.Keywords
This publication has 4 references indexed in Scilit:
- Transient phase of adenosine triphosphate hydrolysis by myosin, heavy meromyosin, and subfragment 1Biochemistry, 1977
- Structure and Function of the Two Heads of the Myosin MoleculeThe Journal of Biochemistry, 1976
- Structure and Function of the Two Heads of the Myosin MoleculeThe Journal of Biochemistry, 1976
- The Contractile and Control Sites of Natural ActomyosinThe Journal of general physiology, 1967