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- W1966950830 abstract "A method is presented for the micro-scale isolation and characterization of erythrocyte membrane Ca2+-ATPase from small samples (7 mL) of whole human blood. Ca2+-ATPase isolated by this technique was more than 92% pure and showed calcium-activation characteristics similar to enzyme purified by standard macroscale procedures—viz maximal velocity of activation (Vca2+) = 15.5 ± 1.2 μmol ATP hydrolysed/mg/min, and reciprocal of apparent affinity (Kca2+) = 0.73 ± 0.15 μM free calcium (mean ± SEM; n = 9). Using the isolation procedure described, purified Ca2+-ATPase could be prepared and assayed in a single working day. When the calcium-activation kinetics of cystic fibrosis erythrocyte membrane Ca2+-ATPase were reassessed using enzyme purified by this technique, Vca2+ and Kca2+ were not significantly different from normal values." @default.
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- W1966950830 date "1991-11-01" @default.
- W1966950830 modified "2023-10-16" @default.
- W1966950830 title "Purification and analysis of erythrocyte membrane Ca2+-ATPase from small samples of patient blood: Application to cystic fibrosis" @default.
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- W1966950830 doi "https://doi.org/10.1016/0160-5402(91)90042-4" @default.
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