Myofibrillar ATPase activity and mechanical performance of skinned fibres from rabbit psoas muscle.
1. The relationship between energy turnover and mechanical performance was investigated in chemically skinned single fibres from rabbit psoas muscle at 15 degrees C, pH = 7.1, with MgATP, 5 mM; free Mg2+, 1 mM; ionic strength, 200 mM and sarcomere length, 2.4 microns by measuring force production and myofibrillar ATP turnover during isometric contractions as well as during repetitive changes in length. ATP hydrolysis was stoichiometrically coupled to the breakdown of NADH, which was measured photometrically via the absorption of near UV light at 340 nm. 2. Force and ATPase activity were measured during square-wave length changes of different amplitudes (1-10% of the fibre length, Lo) and different frequencies (2.5-167 Hz). The average force during the length changes was less than the isometric value and decreased with increasing amplitude and frequency. At full activation (pCa 4.5), the isometric ATP turnover rate (+/- S.E.M.) was 2.30 +/- 0.05 s-1 per myosin head. ATP turnover increased monotonically with increasing amplitude as well as with increasing frequency until saturation was reached. The greatest increase observed was 2.4 times the isometric value. 3. Force and ATPase activity were also determined for ramp shortenings followed by fast restretches. The average force decreased with increasing shortening velocity in a hyperbolic fashion. The ATP turnover increased with ramp velocity up to 0.5 L0 s-1 and stayed almost constant (at 2.2 times the isometric value) for larger velocities. 4. Isometric force and ATPase activity both decreased as the calcium concentration was decreased. They did not vary in proportion at low Ca2+ concentrations, but this could largely be accounted for by the presence of a residual, Ca(2+)-dependent, membrane-bound ATPase. At high calcium concentrations ATPase activity during square-wave length changes was higher than the isometric value, but at low calcium concentrations (pCa > 6.1), the ATPase activity during the length changes decreased below the isometric value and reached a minimum of 40% of the isometric level. 5. ATPase activity and average force obtained during changes in length show a high, movement protocol-independent correlation. During the length changes the rate of ATP turnover divided by the average force level (tension cost) was larger than the isometric tension cost. The largest value found, for 10% length changes at 23 Hz, was 17 times the tension cost under isometric conditions.(ABSTRACT TRUNCATED AT 400 WORDS)
Potma
E J
EJ
Laboratory for Physiology, Free University, Amsterdam, The Netherlands.
Stienen
G J
GJ
Barends
J P
JP
Elzinga
G
G
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000502:physiology; D004734:Energy Metabolism / Q000502:physiology; D066298:In Vitro Techniques; D007537:Isometric Contraction / Q000502:physiology; D007700:Kinetics; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000201:enzymology* / Q000502:physiology*; D009210:Myofibrils / Q000201:enzymology* / Q000502:physiology*; D016658:Psoas Muscles / Q000166:cytology / Q000201:enzymology / Q000502:physiology; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D002118:Calcium