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Direct measurement of newly synthesized ATP dissociation kinetics in sarcoplasmic reticulum ATPase

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6156432

Incubation of SR vesicles with CaS and (TSP)acetylphosphate, yields steady state levels of (TSP)phosphorylated enzyme (ATPase) intermediate and high concentrations of CaS in the lumen of the vesicles. At this time, addition of ADP (and EGTA to lower the CaS concentration in the medium outside the vesicles) results in single cycle formation of (el-TSP)ATP by transfer of (TSP)phosphate from the enzyme intermediate to ADP. The phosphoenzyme decay and ATP formation exhibit a fast component within the first 20 msec following addition of ADP, and a slower component reaching an asymptote in approximately 100 msec. They have now measured by a rapid filtration method the fraction of newly synthesized ATP which is bound to the enzyme, as opposed to the fraction dissociated into the medium. They find that nearly all the ATP formed during the initial burst is still bound to the enzyme within the initial 20 msec of reaction. Dissociation of newly synthesized ATP occurs then with approximately 13 sec rate constant, permitting reequilibration of the system and further formation of ATP. The rate limiting effect of ATP dissociation and other partial reactions on the slow component of single cycle ATP synthesis is evaluated by appropriate kinetic simulations.

Research Organization:
Univ. of Maryland School of Medicine, Baltimore
OSTI ID:
6156432
Report Number(s):
CONF-870644-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 46:6; ISSN FEPRA
Country of Publication:
United States
Language:
English