The Mechanochemistry of Muscular Contraction
The Mechanochemistry of Muscular Contraction
复制标题
肌肉收缩的力学化学
DOI:
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发表时间:
1960
期刊:
影响因子:
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通讯作者:
A. Siger
中科院分区:
文献类型:
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作者:
F. D. Carlson;A. Siger
The dependence of PC1 and ATP1 dephosphorylation on the number of isometric twitches in the iodoacetate-nitrogen-poisoned muscle has been examined. There is no net dephosphorylation of adenosinetriphosphate. PC dephosphorylation varies linearly with the number of twitches and produces equivalent amounts of C1 and P1i.1 Iodoacetate concentrations which block the enzyme, creatine phosphokinase, render the muscle non-contractile. A value of 0.286 µmole/gm. for the amount of PC split per twitch is obtained which gives a value of -9.62 kcal./mole for the "physiological" heat of hydrolysis of PC in agreement with expectations based on thermochemical data. In a single maximal isometric twitch it is estimated that 2 to 3 PC molecules are dephosphorylated per myosin molecule, or 1 per actin molecule. The results support the view that under the conditions of these experiments PC dephosphorylation is the net energy yielding reaction. The in vivo stoichiometry of the mechano-chemistry of contraction revealed by these studies on the one hand, and the known stoichiometry of actin polymerization and its coupling to the creatine phosphokinase system on the other are strikingly similar and strongly suggest that the reversible polymerization of actin is involved in a major way in the contraction-relaxation-recovery cycle of muscle.