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Effects of calcium and ionic strength on shortening velocity and tension development in frog skinned muscle fibres.
Author(s) -
Julian F J,
Moss R L
Publication year - 1981
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.1981.sp013580
Subject(s) - calcium , tension (geology) , biophysics , ionic bonding , chemistry , muscle contraction , anatomy , materials science , biology , composite material , ion , ultimate tensile strength , organic chemistry
1. The influence of Ca2+ concentration and ionic strength on the maximum velocity of shortening (Vmax) and the tension generating capability of frog skinned muscle fibres has been studied at temperatures between 1 and 10 degrees C. 2. Fibre segments were mounted between a force transducer and servo motor, where they could be viewed and photographed through a microscope. Segments in which the striations became non‐uniform during activation were discarded. 3. Velocity was obtained as a function of load by stepping the tension to values less than the steady isometric tension. Vmax was then determined by an extrapolation technique. Vmax was also obtained using a second, independent method by measuring the times required to take up various amounts of slack imposed on the segments. 4. Vmax was significantly influenced by the Ca2+ concentration, decreasing by about one half when the Ca2+ concentration was reduced to give steady tensions less than half‐maximal. 5. Vmax was not influenced by changes in ionic strength, in the range 0.09‐0.18 M. Steady tension was found to increase as ionic strength was decreased in the same range. 6. These results indicate that the effect of changes in ionic strength is to alter the numbers or stiffness of attached cross‐bridges, while there is no apparent influence of ionic strength on the steady‐state kinetics of the actin‐myosin interaction during unloaded shortening. The mechanism responsible for the influence of Ca2+ on Vmax is unknown, though possible sites of action for Ca2+ are discussed.