Abstract
Environmental variances were noted around the rapidly reacting SH-1 thiol of ventricular versus atrial myosin, based on electron paramagnetic resonance studies. Further studies, in which either SH-1 or SH-1 + SH-2 thiols were modified with N-ethylmaleimide, indicated the importance of the SH-2 moiety of both isozymes for generation of tension, when analyzed as synthetic actomyosin threads. Comparative EPR studies showed that the spin label was more strongly immobilized when complexed to ventricular SH-1 thiol as compared to when it was complexed to atrial myosin. Likewise, addition of PPi, ATP or ADP created a greater mobility in the spin label when added to ventricular spin-labeled myosin as compared to that of atrial myosin. comparative studies of spin-labeled actomyosin versus myosin analyzed at different EPR power settings also demonstrated disparaties surrounding the SH-1 thiol between the two myosin isozymes.
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.
