Phosphate burst in permeable muscle fibers of the rabbit

Biophysical Journal
M A Ferenczi

Abstract

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).

References

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Citations

Jan 29, 2000·Journal of the American Psychoanalytic Association·P T Hoffer, A Hoffer
Jul 19, 1996·The Journal of Biological Chemistry·J SierraltaB A Suárez-Isla
Jan 15, 1990·Physical Review. B, Condensed Matter·O O AwadelkarimB Monemar
Apr 29, 1992·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·M R Webb
Sep 2, 1998·The American Journal of Physiology·S J SimnettC C Ashley
Apr 4, 2000·Physiological Reviews·A M GordonM Regnier
Dec 1, 1991·Journal of Muscle Research and Cell Motility·G J Stienen, M A Ferenczi
May 1, 1992·The American Journal of Physiology·N C Millar, E Homsher
Apr 12, 1994·Biochemistry·C HerrmannT Barman

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