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- W51969263 abstract "This chapter examines the structural studies, molecular cloning and localization of the plasma membrane Ca 2+ -pumping ATPase. The action of calcium ion as an intracellular regulatory signal requires a complex set of biochemical processes including Ca 2+ release or influx in response to stimuli, binding to intracellular receptors and removal of regulatory calcium to terminate the response. The latter process occurs as a result of membrane bound ion pumps that can translocate Ca 2+ either into protected compartments within the cell or through the plasma membrane to the external environment. It is observed that the ion translocases that couple the hydrolysis of ATP to Ca 2+ pumping are most important in restoring intracellular Ca levels to the submicromolar range required for the resting. All studies of purified membrane Ca 2+ -ATPase were performed with the enzyme purified to homogeneity from human erythrocyte membranes. This preparation was also utilized to prepare immunoreagents used for both localization and molecular cloning studies in rat and bovine species, respectively. High titer polyclonal antihuman ATPase antibodies were raised in New Zealand rabbits by standard immunization regimes with Freunds adjuvant and purified from the resulting high titer hyperimmune sera by adsorption to antigen immobilized on CaM-Sepharose or following transfer to nitrocellulose." @default.
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- W51969263 date "1987-01-01" @default.
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- W51969263 title "Structural Studies, Molecular Cloning, and Localization of the Plasma Membrane Ca2+-pumping ATPase11Supported by N.I.H. grant No. NS-21868 (T.C.V.), a DOD Predoctoral Fellowship (P.B.) and the U.K. College of Medicine PSP fund (T.C.V./R.E.R.)." @default.
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- W51969263 doi "https://doi.org/10.1016/b978-0-12-521040-9.50095-4" @default.
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