Abstract
Using myosin light chains and tropomyosin subunits as representative myofibrillar proteins, we have characterized their isoprotein forms and also correlated them with the accumulation of the corresponding mRNAs during development of a fast muscle in chicken, viz, pectoralis. Both slow and fast myosin light chain isoforms, except fast myosin light chain LC 3, and the two subunits of tropomyosin are present in early embryonic muscle. During development, the slow myosin light chains and β-tropomyosin appear in reduced amounts in pectoralis muscle and finally they disappear in adult muscle. Translation studies with total cellular RNA from developing muscle indicates that while the protein levels of the above isoforms, in general, correlate with the accumulation of corresponding mRNAs, for LC 3, additional post-transcriptional control appears to modulate the expression of this isoprotein skeletal muscle development in vivo.
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.
