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Articles in PresS, published online ahead of print June 6, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00274.2002
Submitted on March 28, 2002
Accepted on June 4, 2002
1 Molecular Physiology & Biophysics, University of Vermont, Burlington, VT, USA
2 Molecular Cardiovascular Biology, Children's Hospital, Cincinnati, OH, USA
* To whom correspondence should be addressed. E-mail: warshaw{at}physiology.med.uvm.edu.
Two myosin isoforms are expressed in myocardium; 
homodimers (V1) and ßß homodimers (V3). V1 exhibits higher velocities and myofibrillar ATPase activities compared to V3. We, too, observed this for cardiac myosin from normal (V1) and propylthiouracil-treated mice (V3). Actin velocity in a motility assay (Vactin) over V1 myosin was twice that of V3 as was the myofibrillar ATPase. Myosin's average force (Favg) was similar for V1 and V3. Comparing Vactin and Favg across species for both V1 and V3, mouse V1 has greater Vactin and Favg compared to rabbit V1 (47). Mouse V3 Vactin was twice that of rabbit Vactin. To understand myosin's molecular structure and function, we compared - and ß-cardiac myosin sequences from rodents and rabbits. The rabbit - and ß-cardiac differed by 8 and 4 amino acids, respectively, when compared to rodents. These residues are localized to both the motor domain and rod. These differences in sequence and mechanical performance may be an evolutionary attempt to match a myosin's mechanical behavior to the heart's power requirements.
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