SUMMARYRecently we have shown that actomyosin ATPase activity decreases with age when measured under appropriate conditions (Yoshida K et al, Age 12: 97-102, 1989). Many previous studies, which examined changes in ATPase activity in myosin, actomyosin, or myofibrils under pathological states, ignored the age-related changes. In this study actomyosin was isolated from myocardia of middle-aged subjects (37-49 years old) and examined for ATPase activity under various conditions and protein composition. Proteolysis of myosin and troponin was more frequently observed in ischemic heart disease (IHD) subjects than in non-IHD subjects. The proteolysis was associated with a decrease in Ca2+ sensitivity of Mg2+-ATPase activity and enhanced stimulation of Ca2+-ATPase activity with a sulfhydryl reagent, N-ethylmaleimide. Hypertrophy appeared not to significantly affect ATPase activity.Additional Indexing Words: Actomyosin Human myocardium ATPase activity Proteolysis Ischemic heart disease Y modifying conventional assay conditions, we and others have found age-dependent changes in the actomyosin ATPase activity of human myocardia.1)-4) Recently we observed that myosin heavy chain and troponin in the actomyosin of some subjects, particularly middle-aged and elderly persons, showed proteolysis of myosin and troponin.5) Malhotra et al reported that purified myosin from aged subjects contained proteolytic products of the heavy chain, while that from young subjects did not.6) The proteolysis might alter the ATPase activity. These findings led us to the "old" question of whether or not certain pathological states affect actomyosin (or myofibril or myosin) ATPase activity.7)-12) The question has not been answered properly because age has not been considered and the assay conditions for ATPase activity have been limited in previous studies. It seemed to us that