Force measurements in skinned muscle fibres.
1. Isometric force was measured in skinned segments of frog semitendinosus muscle fibres exposed to solutions in which the calcium ion concentration was controlled with EGTA.2. The threshold for force development, calculated from an apparent stability constant for the CaEGTA complex of 10(6.69)M(-1) at pH 7.0, was generally close to pCa 7.5. Maximum force was reached at about pCa 6.0.3. Maximum force is proportional to the cross-sectional area of the fibres.4. The rate of force development was slower than that expected from simple diffusion of a substance from the bathing solution into the fibre. The delay appears to be due to slow equilibration of the EGTA buffer system during calcium uptake by the sarcoplasmic reticulum.5. Addition of deoxycholate (DOC) to the bathing solution produced a reversible increase in the rate of force development. The steady force was also increased for values of pCa that gave less than maximum force, which shifted the force-pCa relation toward lower calcium concentrations by about 0.5 pCa unit.6. The length-force relation in partially activated preparations is similar to that reported for electrically activated intact fibres. This result suggests that in the region of myofilament overlap the affinity of the binding sites for calcium is uniform along the length of the calciumbinding myofilament.
D000818:Animals; D001001:Anura; D001647:Bile Acids and Salts / Q000494:pharmacology; D001665:Binding Sites; D002118:Calcium / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology*; D004558:Electric Stimulation; D004987:Ethers / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007094:Imides / Q000494:pharmacology; D066298:In Vitro Techniques; D009119:Muscle Contraction / Q000187:drug effects; D009132:Muscles / Q000502:physiology; D009210:Myofibrils / Q000502:physiology*; D012508:Sarcolemma / Q000502:physiology; D013997:Time Factors
D001647:Bile Acids and Salts; D004987:Ethers; D007094:Imides; D002118:Calcium