Abstract
A method is presented for the micro-scale isolation and characterization of erythrocyte membrane Ca 2+-ATPase from small samples (7 mL) of whole human blood. Ca 2+-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 (V ca2+) = 15.5 ± 1.2 μmol ATP hydrolysed/mg/min, and reciprocal of apparent affinity (K ca2 +) = 0.73 ± 0.15 μM free calcium (mean ± SEM; n = 9). Using the isolation procedure described, purified Ca 2+-ATPase could be prepared and assayed in a single working day. When the calcium-activation kinetics of cystic fibrosis erythrocyte membrane Ca 2+-ATPase were reassessed using enzyme purified by this technique, V ca2+ and K ca2+ were not significantly different from normal values.
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