2
Views
1
CrossRef citations to date
0
Altmetric
Original Article

Identification of a Spectroscopic Marker for the Ca2+-Binding Site of (Ca2+ + Mg2+)-ATPase of Sarcoplasmic Reticulum in the Occluded State

&
Pages 61-67 | Accepted 27 Jun 1990, Published online: 09 Jul 2009

References

  • Banerjee R., Epstein M., Kandrich M., Zimmiack P., Racker E. A new method of preparing Ca2+–ATPase from sarcoplasmic reticulum: Extraction with octylglucoside. Membrane Biochem. 1979; 2: 283–296
  • Dupont Y. Occlusion of divalent cations in the phosphorylated calcium pump of sarcoplasmic reticulum. Eur. J. Biochem. 1980; 109(l)231–238
  • Gangola P., Shamoo A. E. Synthesis and characterization of peptide segment of (Ca2+ + Mg2+)–ATPase—A candidate for Ca2+ transport site. J. Biol. Chem. 1986; 261: 8601–8603
  • Gangola P., Shamoo A. E. Characterization of (Ca2+ + Mg2+)–ATPase of sarcoplasmic reticulum by laser–excited europium luminescence. Eur. J. Biochem. 1987; 162: 357–363
  • Herrmann T. R., Jayaweera A. R., Shamoo A. E. Interaction of europium(III) with phospholipid vesicles as monitored by laser–excited europium(III) luminescence. Biochemistry 1986; 25: 5834–5838
  • Herrmann T. R., Shamoo A. E. Estimation of inter–binding–site distance in sarcoplasmic reticulum (Ca2+ + Mg2+)–ATPase under occluded and non–occluded conditions. Mol. Cell. Biochem. 1988; 8: 55–58
  • Lockwich T., Douglass C., Shamoo A. E. Uncoupling of Ca2+ occlusion from ATP hydrolysis activity in sarcoplasmic reticulum. Eur. J. Biochem. 1990, submitted
  • Lowry O. K., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
  • MacLennan D. H. Purification and properties of an adenosine triphosphate from sarcoplasmic reticulum. J. Biol. Chem. 1970; 245: 4508–4518
  • Racker E. Reconstitution of calcium pump with phospholipids and a purified calciumadenosine triphosphatase from sarcoplasmic reticulum. J. Biol. Chem. 1972; 247: 8198
  • Saito K., Imamura Y., Kawakita M. Effect of temperature and added ligands on the susceptibility of Ca2+, Mg2+– ATPase of the sarcoplasmic reticulum to trypsin. J. Biochem. 1984; 95: 1297–1304
  • Scott T. L., Shamoo A. E. Disruption of energy transduction in sarcoplasmic reticulum. J. Membrane Biol. 1982; 64: 137–144
  • Scott T. L., Shamoo A. E. Distinction of the roles of the two high–affinity calcium sites in the functional activities of the Ca2+ –ATPase of sarcoplasmic reticulum. Eur. J. Biochem. 1984; 143: 427–436
  • Shamoo A. E., Herrmann T. R. Tertiary structure of the (Ca2+ + Mg2+)–ATPase probed by laser–pulsed lanthanide luminescence spectroscopy. Proc. Int. Symp. Adv. Biotechnology of Membrane Ion Transport. Sept., 19–201988. vol. 51: 125–133
  • Shamoo A. E., Herrmann T. R., Gangola P., Joshi J. B. (1987) Biophysical Aspects of Calcium Transport Sites in Skeletal and Cardiac Sarcoplasmic Reticulum (Ca2+ + Mg2+)–ATPase. Proc. Symp. Heart Metabolism in Health and Disease. July, 8–111986, 221–241
  • Shamoo A. E., Joshi N. B. Regulation of the Peptide Region of the Calcium and ATP Sites of the Calcium Pump Protein. Proc. Third Int. Workshop on Calcium and Phosphate Transport across Biomembranes. In Progress in Clinical and Biological Research. 1987; 252: 141–148

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.