Equilibrium and Kinetic Studies of Calcium Transport and ATPase Activity in Sarcoplasmic Reticulum
Open Access
- 1 August 1982
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 37 (7-8) , 685-691
- https://doi.org/10.1515/znc-1982-7-819
Abstract
A number of equilibrium and kinetic mesurements are presented to characterize the partial reactions of the ATPase and transport cycle in [rabbit] sarcoplasmic reticulum vesicles. The cycle begins with Ca and nucleotide binding on sites available on the outer surface of the vesicles. A phosphorylated enzyme intermediate is then formed and the Ca sites are subjected to a change in their orientation and their affinity for Ca. Steps involved in Ca release on the inner side of the vesicles are rate limiting for the cycle and are followed by hydrolytic cleavage of the intermediate with release of Pi and recycling of the enzyme.Keywords
This publication has 2 references indexed in Scilit:
- Occlusion of Divalent Cations in the Phosphorylated Calcium Pump of Sarcoplasmic ReticulumEuropean Journal of Biochemistry, 1980
- The nature of the cardiac relaxing factorBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1967