Synthetic Monoacylphospholipids as Reactivators of the Calcium-Dependent ATPase of Enzymatically Delipidated Sarcoplasmic Membranes
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چکیده
منابع مشابه
Low affinity calcium binding sites of the calcium transport ATPase of sarcoplasmic reticulum membranes.
Calcium binding sites having low affinity constants of less than 10(3) M-1 were titrated in native sarcomplasmic reticulum vesicles as well as in lipid deprived membranes and in the isolated calcium transport ATPase. Short time calcium binding measurements and the determination of the calcium binding heat allow to distinguish low affinity calcium binding sites located on the external surface of...
متن کاملRole of phospholipids in the calcium-dependent ATPase of the sarcoplasmic reticulum. Enzymatic and ESR studies with phospholipid-replaced membranes.
Three types of partially purified ATPase enzymes having different phospholipid contents and compositions have been prepared: (a) an enzyme whose phospholipid moiety has been replaced predominantly by dioleoyl lecithin (DOL-enzyme), with about the same phospholipid content as the original sarcoplasmic reticulum, (b) dipalmitoyl lecithin-replaced enzyme whose phospholipid content is 30% of that o...
متن کاملRole of Phospholipids in the Calcium-dependent ATPase of the Sarcoplasmic Reticulum
Three types of partially purified ATPase enzymes having different phospholipid contents and compositions have been prepared: (a) an enzyme whose phospholipid moiety has been replaced predominantly by dioleoyl lecithin (DOL-enzyme), with about the same phospholipid content as the original sarcoplasmic reticulum, (b) dipalmitoyl lecithin-replaced enzyme whose phospholipid content is 30% of that o...
متن کاملCalcium-dependent calcium occlusion in the sarcoplasmic reticulum Ca2+-ATPase. Its enhancement by phosphorylation of the enzyme.
45Ca2+-40Ca2+ exchangeability of 45Ca bound to the calcium transport sites of unphosphorylated sarcoplasmic reticulum Ca2+-ATPase at equilibrium has been found to be heterogeneous: Half of the bound calcium is [Ca2+]-dependent in a slowly exchangeable (k less than 0.3 s-1), "occluded" state in the Ca2+-ATPase, and the other calcium is [Ca2+]-independent in a rapidly exchangeable (k approximatel...
متن کاملAcetyl phosphate as a substrate for the calcium ATPase of sarcoplasmic reticulum.
Acetyl phosphate is hydrolyzed by the calcium ATPase of leaky sarcoplasmic reticulum vesicles from rabbit skeletal muscle with Km = 6.5 mM and kcat = 7.9 s-1 in the presence of 100 microM calcium (180 mM K+, 5 mM MgSO4, pH 7.0, 25 degrees C). In the absence of calcium, hydrolysis is 6% of the calcium-dependent rate at low and 24% at saturating concentrations of acetyl phosphate. Values of K0.5 ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2005
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1981.tb06390.x