Abstract

Immunological, structural and enzymatic characteristics of atrial and ventricular myosin from euthyroid rabbits were analyzed and compared with ventricular myosin from hyperthyroid animals. (1) Specific antibodies against bovine atrial myosin were found to react selectively in double-immunodiffusion and enzyme immunoassay with both rabbit atrial myosin and ventricular myosin from thyroxine-treated animals. These specific anti-bovine atrial myosin antibodies reacted with the heavy chains of thyrotoxic ventricular myosin when examined by enzyme immunoassay combined with SDS-polyacrylamide gel electrophoresis. (2) In one-dimensional SDS-polyacrylamide gel electrophoresis, no difference could be demonstrated in the light chain pattern of ventricular myosin from euthyroid and hyperthyroid rabbit hearts. One-dimensional analysis of myosin heavy chains after chymotryptic digestion in the presence of SDS showed significant differences between the two ventricular myosins. Also, the peptide maps from atrial myosin resembled the pattern of peptides found with ventricular heavy chains from hyperthyroid rabbits. The steady state rate, the alkali stability and the pH sensitivity of Ca 2+-ATPase activity of thyrotoxic ventricular myosin were very similar to those of atrial myosin. (3) These results provide direct immunochemical and biochemical evidence for the existence of an atrial-like isomyosin in thyrotoxic rabbit ventricles.

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