The state of water associated with the phosphoenzyme of the Ca-ATPase of sarcoplasmic reticulum
- 1 November 1987
- journal article
- research article
- Published by Elsevier in Bioelectrochemistry and Bioenergetics
- Vol. 17 (3) , 473-487
- https://doi.org/10.1016/0302-4598(87)80055-7
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- The Solvent Properties of Water in Desalination MembranesJournal of Macromolecular Science: Part A - Chemistry, 1986
- Relationship between pump and leak: Part II. A model of the Na,K-ATPase functioning both as pump and leakBioelectrochemistry and Bioenergetics, 1985
- The relationship between pump and leak: Part 1. Application of the Butler-Volmer equationBioelectrochemistry and Bioenergetics, 1985
- Relationship between pump and leakBioelectrochemistry and Bioenergetics, 1985
- Studies of the interactions of 2‘,3‘-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site.Journal of Biological Chemistry, 1984
- Evaluation of H2O activity in the free or phosphorylated catalytic site of Ca2+‐ATPaseFEBS Letters, 1983
- A possible mechanism for the Na,K-ATPaseJournal of Theoretical Biology, 1982
- A possible mechanism for the Ca-ATPase of sarcoplasmic reticulumJournal of Theoretical Biology, 1982
- The effect of the Ca2+-ATPase of sarcoplasmic reticulum upon activities of Na+, K+, and H3O+ ions.Journal of Biological Chemistry, 1980
- The mechanism of water transport in membranesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1977