Abstract
1. 1. Two types of myosins with phosphorylated and dephosphorylated myosin light chains were prepared from Drosophila flies. The former had ATPase ( Ca 2+- and Mg 2+-activated ) activities twice those of the latter. 2. 2. The myosin phosphorylated with crude myosin light chain kinase from flies showed ATPase ( Ca 2+- and Mg 2+-activated ) activaties twice those of the dephosphorylated myosin. 3. 3. It is suggested that phosphorylation of myosin light chains several hours after emergence stimulates myosin ATPase activity so as to facilitate the flight function of the fruitfly.
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 callMore From: Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
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.
