Abstract
The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine. The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.
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.
