Abstract
Disodium pyrophosphate at 10 mM concentration, was effective in dissociating myosin and actin from actomyosin in walleye pollock ( Theragra chalcogramma) surimi and red bulleye ( Priacanthus macracanthus) surimi. After Sepharose 2B gel filtration, cathepsin L contained in the actomyosin was obviously non-binding to myosin. Actomyosin from carp ( Cyprinus carpio) muscle was not dissociated in pyrophosphate solution in the absence of MgCl 2 and it was successfully dissociated by 10 mM pyrophosphate in the presence of 2 mM MgCl 2. Cathepsin L in carp actomyosin was shown to be much more complicated than that in the above two surimis. After Sepharose 2B gel filtration, there were two activity peaks of cathepsin L in carp, one almost corresponding with actomyosin, the other obviously separated from actomyosin. Both of the peaks were non-binding to myosin.
Sign-in/Register to access full text options 
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.
