The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion

The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion

Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and...

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Veröffentlicht in:FEBS letters 1990-01, Vol.260 (1), p.83-84
Hauptverfasser: Khananshvili, D., Myung, J., Kolouch, R., Jencks, W.P.
Format: Artikel
Sprache:eng
Schlagworte:
Animals
ATPase, calcium
Binding Sites - drug effects
Binding, Competitive
Calcimycin - pharmacology
Calcium
Calcium - pharmacology
Calcium-Transporting ATPases - antagonists & inhibitors
Exact sciences and technology
Inhibition
Magnesium - pharmacology
Mathematical analysis
Mathematics
Potential theory
Rabbits
Sarcoplasmic Reticulum - enzymology
Sciences and techniques of general use
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Zusammenfassung:Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A‐P·Ca1.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)80071-P