title: The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion.
abstract: 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 microM 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.
authors: Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
authors: D
authors: D
authors: Khananshvili
authors: J
authors: J
authors: Myung
authors: R
authors: R
authors: Kolouch
authors: W P
authors: WP
authors: Jencks
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001667:Binding, Competitive; D000001:Calcimycin / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology*; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D008274:Magnesium / Q000494:pharmacology; D008433:Mathematics; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
chemical_list: D000001:Calcimycin; D000252:Calcium-Transporting ATPases; D008274:Magnesium; D002118:Calcium