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The synthesis rates of total heart protein and of sarcoplasmic and myofibrillar protein fractions have been determined by perfusion of isolated rat hearts with [(14)C]tyrosine at constant specific radioactivity. In hearts perfused without insulin, both myofibrillar and sarcoplasmic proteins were synthesized at a fractional rate of 10-11% per day. This corresponds to a half-life for synthesis of about 7 days. The effect of added insulin was to increase the rate of heart-protein synthesis to a half-life of 3-4 days. With hearts perfused via the left atrium and performing external work, there was a rise in the specific radioactivity of intracellular free tyrosine, and the half-life for synthesis of proteins was 3-4 days. The extent of labelling of individual myofibrillar proteins was estimated after polyacrylamide-gel electrophoresis of solubilized myofibrils in the presence of sodium dodecyl sulphate. No particular protein showed an unusually high or low specific radioactivity after labelling in perfusion. Insulin caused a general increase in labelling of all the proteins analysed.

Synthesis rates of protein in the Langendorff-perfused rat heart in the presence and absence of insulin, and in the working heart