Conformational states of sarcoplasmic reticulum Ca2+-ATPase as studied by proteolytic cleavage
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/BF01868432.pdf
Reference46 articles.
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2. Andersen, J.P., Fellmann, P., Møller, J.V., Devaux, P.F. 1981. Immobilization of a spin-labeled fatty acid chain covalently attached to Ca2+-ATPase from sarcoplasmic reticulum suggests an oligomeric structure.Biochemistry 20:4928–4936
3. Andersen, J.P., Lassen, K., Møller, J.V. 1985. Changes in Ca2+ affinity related to conformational transitions in the phosphorylated state of soluble monomeric Ca2+-ATPase from sarcoplasmic reticulum.J. Biol. Chem. 260:371–380
4. Andersen, J.P., Møller, J.V., Jørgensen, P.L. 1982. The functional unit of sarcoplasmic reticulum Ca2+-ATPase: Active site titration and fluorescence measurements.J. Biol. Chem. 257:8300–8307
5. Andersen, J.P., Skriver, E., Mahrous, T.S., Møller, J.V. 1983. Reconstitution of sarcoplasmic reticulum Ca2+-ATPase with excess lipid: Dispersion of the pump units.Biochim. Biophys. Acta 728:1–10
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