Pflügers Archiv

, Volume 377, Issue 2, pp 119–124 | Cite as

The relationship of mechanicalVmax to myosin ATPase activity in rabbit and marmot ventricular muscle

  • Burt B. Hamrell
  • Robert B. Low
Heart, Circulation, Respiration and Blood; Environmental and Exercise Physiology

Abstract

Papillary muscle mechanics and ventricular myosin calcium-activated ATPase activity were measured in the same heart as a function of temperature (8–28°) in rabbits and marmots, in order to examine further the hypothesis that the velocity of cardiac muscle shortening at zero load (Vmax) is correlated with myosin ATPase activity. There was a similarQ10 forVmax in each muscle type, as measured with isotonic afterloaded quick-releases at 30–33% time-to-peak tension; the calcium activated ATPase of myosin in the two muscle types also was similar. The least squares linear regression of rabbitVmax on calcium-activated myosin ATPase activity was the same as in the marmot, so all the data were pooled to yield a linear regression (Y=0.47+3.82X) with a high correlation between the two variables [r=0.95,P<0.01 (ANOV)]. Furthermore, the correlation proved to be predictive of cardiacVmax and myosin ATPase activity levels in other experiments where these two measurements decreased below normal as a result of hypertrophic growth. Consequently, the quantitative relationship betweenVmax and myosin ATPase defined here may prove to be predictive of the ability of cardiac muscle to release bond energy.

Key words

Vmax Myosin ATPase Force-velocity Temperature Myocardium 

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Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Burt B. Hamrell
    • 1
  • Robert B. Low
    • 1
  1. 1.Department of Physiology and BiophysicsUniversity of Vermont College of MedicineBurlingtonUSA

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