Abundance of the Ca2+-pumping ATPase in pig erythrocyte membranes.
نویسندگان
چکیده
The Ca2+-pumping ATPase (Ca2+-ATPase) was purified from human and pig erythrocyte membranes by calmodulin affinity chromatography in the presence of phosphatidylcholine. The amount of enzyme present in pig erythrocytes is at least 7 times greater than that isolated from human erythrocyte ghosts. However, the properties of the enzyme from the two species are similar in many respects.
منابع مشابه
Inhibitory antibodies to plasmalemmal Ca 2 + - transporting
Antibodies directed against the purified calmodulin-binding (Ca2++ Mg2+)-ATPase [(Ca2+ + Mg2+)dependent ATPase] from pig erythrocytes and from smooth muscle of pig stomach (antral part) were raised in rabbits. Both the IgGs against the erythrocyte (Ca2++ Mg2+)-ATPase and against the smooth-muscle (Ca2+ + Mg2+)-ATPase inhibited the activity of the purified calmodulin-binding (Ca2++ Mg2+)-ATPase ...
متن کاملEvidence for the presence in smooth muscle of two types of Ca2+-transport ATPase.
Membrane fractions prepared from smooth muscle of the pig stomach (antral part) contain two Ca2+-dependent phosphoprotein intermediates belonging to different Ca2+-transport ATPases. These alkali-labile phosphoproteins can be separated by electrophoresis in acid medium. The 130 kDa phosphoprotein resembles a corresponding protein in the erythrocyte membrane, whereas the 100 kDa protein resemble...
متن کاملAcidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase.
The purified Ca2+-pumping ATPase of human erythrocyte membranes (Niggli, V., Adunyah, E. S., Penniston, J. T., and Carafoli, E. (1981) J. Biol. Chem. 256, 395-401) can be stimulated, in the absence of calmodulin, by other treatments. 1. A variety of acidic phospholipids (phosphatidylserine, cardiolipin, phosphatidylinositol, and phosphatidic acid) stimulate the Vmax and decrease the Km (Ca2+) o...
متن کاملA high affinity Ca2+ -ATPase in C57 black mouse liver plasma membranes.
Plasma membranes of a cell contain 2 kinds of Ca2÷-extruding mechanisms to maintain [Ca 2÷] of cytoplasm at submicromolar levels, ATP-dependent and extracellular NaLdependent mechanisms. In plasma membranes of several tissues, the ATP-dependent Ca2+-pumps associate with (Ca 2+ + Mg2÷)-ATPase activity [ 1-3 ]. In the case of erythrocyte plasma membrane, a reconstitution study has clearly demonst...
متن کاملAntibodies against erythrocyte Ca2+-transport ATPase specifically inhibit the calmodulin-dependent fraction of the enzyme's activity.
Antibodies against purified Ca2+-transport ATPase from human erythrocytes were raised in rabbits. Immunodiffusion experiments revealed that precipitating antibodies had been developed. The immunoglobulin fraction inhibited solely the calmodulin-dependent fraction of erythrocyte Ca2+-transport ATPase activity, whereas the basal (in the absence of added calmodulin) activity of the enzyme was not ...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 248 1 شماره
صفحات -
تاریخ انتشار 1987