Abstract
Three groups of different-size polysomes obtained from a sucrose gradient analysis of embryonic chick muscle lysate were used as a basis for a cell-free system of protein synthesis. Incubation and characterization of these 3 fractions showed that they were synthesizing myosin, actin, and tropomyosin. Isolation and purification of these molecules indicated that they had been formed in a native configuration. From an analysis of the size of the polysomes and the size of the polypeptide chains in the proteins, it was inferred that all of them are synthesized on mono-cistronic messenger RNA molecules. Changes in the polysomal pattern during embryonic differentiation suggest that actin synthesis is somewhat more predominant initially than myosin synthesis, and that tropomyosin synthesis increases at a later stage than the others.

This publication has 12 references indexed in Scilit: