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• W2037836727 abstract "In striated muscle, force generation and phosphate (Pi) release are closely related. Alterations in the [Pi] bathing skinned fibers have been used to probe key transitions of the mechanochemical coupling. Accuracy in this kind of studies is reduced, however, by diffusional barriers. A new perfusion technique is used to study the effect of [Pi] in single or very thin bundles (1–3 μM in diameter; 5°C) of rabbit psoas myofibrils. With this technique, it is possible to rapidly jump [Pi] during contraction and observe the transient and steady-state effects on force of both an increase and a decrease in [Pi]. Steady-state isometric force decreases linearly with an increase in log[Pi] in the range 500 μM to 10 mM (slope −0.4/decade). Between 5 and 200 μM Pi, the slope of the relation is smaller (∼ −0.07/decade). The rate constant of force development (kTR) increases with an increase in [Pi] over the same concentration range. After rapid jumps in [Pi], the kinetics of both the force decrease with an increase in [Pi] (kPi(+)) and the force increase with a decrease in [Pi] (kPi(−)) were measured. As observed in skinned fibers with caged Pi, kPi(+) is about three to four times higher than kTR, strongly dependent on final [Pi], and scarcely modulated by the activation level. Unexpectedly, the kinetics of force increase after jumps from high to low [Pi] is slower: kPi(−) is indistinguishable from kTR measured at the same [Pi] and has the same calcium sensitivity." @default.
• W2037836727 created "2016-06-24" @default.
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• W2037836727 date "2000-06-01" @default.
• W2037836727 modified "2023-10-15" @default.
• W2037836727 title "The Effect of Inorganic Phosphate on Force Generation in Single Myofibrils from Rabbit Skeletal Muscle" @default.
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• W2037836727 doi "https://doi.org/10.1016/s0006-3495(00)76845-7" @default.
• W2037836727 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1300890" @default.
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