Lumenal Ca 2+ Dissociation from the Phosphorylated Ca 2+ -ATPase of the Sarcoplasmic Reticulum Is Sequential *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 270, Issue: 31, Page: 18271-18276
1995
- 27Citations
- 9Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations27
- Citation Indexes27
- 27
- CrossRef20
- Captures9
- Readers9
Article Description
Once two radioactive Ca 2+ coming from the cytoplasm are bound to the transport sites of the nonphosphorylated ATPase, excess EGTA induces rapid dissociation of both ions, whereas excess nonradioactive Ca 2+ only reaches one of the two bound Ca 2+. This difference has been explained assuming that the two Ca 2+ sites are in a single file channel in which the superficial Ca 2+ is freely exchangeable from the cytoplasm, whereas the deeper Ca 2+ is exchangeable only when the superficial site is vacant. The same experiment was done using phosphorylated ATPase to determine whether Ca 2+ dissociation toward the lumen is sequential as well. Under conditions that allow ADP-sensitive phosphoenzyme to accumulate (leaky vesicles, 5°C, pH 8, 300 mM KCl), we found the same two pools of Ca 2+. Excess EGTA induced dissociation of both ions together with dephosphorylation. Excess nonradioactive Ca 2+ induced the exchange of half the radioactive Ca 2+ without any effect on the phosphoenzyme level. Our results show a close similarity between the transport sites of the nonphosphorylated and the phosphorylated enzymes, although the orientation, affinities, and dissociation rate constants are different.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925817463010; http://dx.doi.org/10.1074/jbc.270.31.18271; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028978212&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/7629146; https://linkinghub.elsevier.com/retrieve/pii/S0021925817463010; https://dx.doi.org/10.1074/jbc.270.31.18271
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know