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

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.