Phosphate burst in permeable muscle fibers of the rabbit.

The transient kinetics of ATP hydrolysis in chemically skinned psoas muscle fibers of the rabbit have been measured. Muscles fibers in the rigor state (absence of nucleotide) were relaxed rapidly by the photochemical release of [2-3H]ATP from caged-ATP (P3-1-(2-nitro)phenylethyl[2-3H]adenosine 5'-triphosphate) in the absence of calcium ions. Rapid freezing of the fiber to stop hydrolysis, followed by analysis of the tritiated nucleotide content allowed the course of the hydrolysis to be determined. The timecourse of ATP hydrolysis was biphasic, with an initial rapid phase occurring at a rate of approximately 60 s-1 at 12 degrees C for fibers exposed to greater than 0.7 mM ATP. The amplitude of the rapid phase was as previously reported (Ferenczi, M. A., E. Homsher, and D. R. Trentham, 1984, J. Physiol. (Lond.)., 352:575-599).