Abstract
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 10mM. Nevertheless, a very small fraction of crossbridges were active at 10mM 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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
