1. In attempting to consolidate the role of ventricular isomyosins in regulating the contractility of the myocardium, actomyosin ATPase and crossbridge kinetics were obtained at 24°C in chemically skinned isometrically contracting cardiac muscles containing V1 and V3 isomyosins. 2. The ATPase activity was measured at various levels of Ca2+ activation by the enzymatic coupling of ATP hydrolysis with the conversion of NADH to NAD+. The crossbridge kinetics were inferred from small‐amplitude perturbations of muscle length and muscle tension, and characterized by the frequency‐domain parameter fmin. 3. The ATPase rates of V1 and V3 muscles obtained at various levels of Ca2+ activation were plotted against the corresponding proportional tensions. The ATPase vs tension plots were linear with slopes of 4.92 nmol/min‐1 per mm per mN and 1.98 nmol/min‐1 per mm per mN, respectively for, V1 and V3 muscles. Individual calculations of ATPase‐to‐tension ratios (nmol/min‐1 per mm per mN) gave corresponding averages of 4.98 ± 0.12 (s.e.m., n = 12) and 2.16 ± 0.12 (s.e.m., n = 10). The myosin isoform induced proportional change in tension cost was accompanied by a similar change in fmin (4.1 ± 0.1 Hz and 1.95 ± 0.03 Hz, means ± s.e.m., for V1 and V3 muscles, respectively). 4. The observations and other published kinetic data are discussed in the context of models of crossbridge cycling. It is suggested that the tension economy of V3 muscle arises principally from an increase in the fraction of time, during the crossbridge cycle, when the crossbridge is exerting force.
|Number of pages||7|
|Journal||Clinical and Experimental Pharmacology and Physiology|
|Publication status||Published - Jul 1995|
- ATPase activity
- complex stiffness
- myosin heavy chains
- skinned cardiac muscle
- tension transient.