The relationship of mechanicalV max to myosin ATPase activity in rabbit and marmot ventricular muscle
- 1 January 1978
- journal article
- research article
- Published by Springer Nature in Pflügers Archiv - European Journal of Physiology
- Vol. 377 (2) , 119-124
- https://doi.org/10.1007/bf00582841
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 (V max) is correlated with myosin ATPase activity. There was a similarQ 10 forV max 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 rabbitV max 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,PV max 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 betweenV max and myosin ATPase defined here may prove to be predictive of the ability of cardiac muscle to release bond energy.This publication has 33 references indexed in Scilit:
- The mechanical characteristics of hypertrophied rabbit cardiac muscle in the absence of congestive heart failure: the contractile and series elastic elements.Circulation Research, 1977
- Structural and functional properties of myosin associated with the compensatory cardiac hypertrophy in the rabbit,Journal of Molecular and Cellular Cardiology, 1976
- Acid‐Base Changes and Excitation‐Contraction Coupling in Rabbit Myocardium. I. Effects on Isometric Tension Development at Different Contraction FrequenciesActa Physiologica Scandinavica, 1975
- The Influence of Temperature on the Force-Velocity Relationship in Rabbit Papillary MuscleActa Physiologica Scandinavica, 1974
- Chemical Studies on Light Chains from Cardiac and Skeletal Muscle MyosinsNature, 1971
- Relationships between Force and Velocity of Shortening in Rabbit Papillary MuscleActa Physiologica Scandinavica, 1971
- Polypeptide chains of intermediate molecular weight in myosin preparationsFEBS Letters, 1971
- Light Chains of MyosinNature, 1969
- ATPase Activity of Myosin Correlated with Speed of Muscle ShorteningThe Journal of general physiology, 1967
- Myothermic experiments on the frog's gastrocnemiusProceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character, 1931