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Myosin ATPase activity is usually considered to reflect the contractile capacity of a given muscle since it correlates with the maximum initial speed of shortening of the unloaded muscle (Vmax). There are several exceptions to this scheme, and it was the goal of this study to determine if the Mg2+-ATPase activity of the covalently bound actomyosin S1 is a more physiological index of contractility. On polyacrylamide gels, the complex obtained after condensation of fast skeletal myosin S1 to skeletal actin is identical to that obtained with myosin S1 from the ventricles of different species, including rat, guinea pig, and human, cross-linked to cardiac or skeletal actin. In every condition, the ATPase activity of the complex is 700-fold higher than that of myosin S1. It correlates linearly with the Vmax both in phylogeny and in conditions in which an isomyosin shift has been reported, such as hypothyroidism and chronic cardiac overload. Such a relation indicates that, in species that already have a low Vmax, a small change in myosin ATPase may induce dramatic consequences in the shortening velocity. Cardiac hypertrophy in humans, where the drop in Vmax is not associated with a myosin change, does not fit into this scheme. The enzymatic activity of the complex is also unmodified in this condition, which shows that, in humans, the myosin ATPase is not a determinant of Vmax and suggests that other mechanisms may be involved. Measurement of this type of ATPase activity provides a new tool to explore contractility biochemically, which is more reproducible and, from a technical point of view, easier to perform than a kinetic assay. It also correlates better with mechanical data obtained with skinned fibers than with those measured on fresh papillary muscles.

circulation research

ATPase activity of the cross-linked complex between cardiac myosin subfragment 1 and actin in several models of chronic overloading. A new approach to the biochemistry of contractility.