Abstract
In this report we have defined three distinct stages of the fast to slow transformation of muscle in terms of the myosin isoenzyme pattern in a non-denaturing gel system. In phase I a rearrangement of fast isoenzymes with no increase in slow isoforms took place. Phase II is characterised by a complex pattern of fast and slow isoenzymes and of isoenzymes of intermediate mobility. Phase III shows full conversion to the slow isoform with residual traces of fast and intermediate components. Changes in myosin light chains, as revealed by two dimensional gel analysis, showed good correlation with their corresponding mRNAs as determined by translation of extracted total RNA in a nuclease treated reticulocyte lysate cell-free system. This suggests that in the fast to slow transformation gene expression is regulated at the level of transcription.
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