Abstract

Myosin was prepared from I g of frog's sartorius muscle and the yield was 20 mg to 30 mg of purified protein per gram wet weight tissue. The extractability of myosin was the same whether the muscle was at rest, in contraction or in fatigue. The adenosine triphosphate concentration was not changed in activity nor in fatigue and thus the extractability of myosin could be related to the unchanged concentration of adenosine triphosphate, but not to the state of activity of the muscle. The adenosine triphosphate activity and the concentration of sulfhydryl groups were the same in pairs of muscles either at rest and in contraction or at test and in fatigue. A fifteen fold decrease in the rate of relaxation of a muscle fatigued by single twitches suggests a progressive change in the relaxing factor system during fatigue.

Full Text
Paper version not known

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 call

Disclaimer: 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.