Premium
The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca 2+ ion
Author(s) -
Khananshvili D.,
Myung J.,
Kolouch R.,
Jencks W.P.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80071-p
Subject(s) - ionophore , calcium , endoplasmic reticulum , chemistry , calcium atpase , atpase , dissociation (chemistry) , biophysics , ion , isotopes of calcium , plasma membrane ca2+ atpase , biochemistry , enzyme , biology , organic chemistry
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 [Mg 2+ ] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca 2+ ions from E‐P·Ca 2 is sequential and that the inhibition arises from the binding of one Ca 2+ to A‐P·Ca 1 .