Semi-purified dog kidney Na+-K+-ATPase was cross-linked with ovalbumin. This immobilized enzyme was able to hydrolyse ATP and this hydrolysis was ouabain-sensitive. It was then used in batch wise affinity chromatography for the detection of endogenous Na+-K+-ATPase inhibitor in human plasma and urine. Ammonium acetate 1 mM washed off the endogenous Na+-K+-ATPase inhibitor from the immobilized enzyme. The inhibitory activity of the eluate from hypertensive plasma was significantly higher (p less than 0.0025, n = 6) than that of normotensive plasma. Similar results were obtained (n = 3) from human urine eluates during salt loading as compared to control urine.
Etude par chromatografie d'affinite' de la variation chez l'homme pendant une surcharge sodee de l'inhibiteur endogene de la Na-K-ATPase [Affinity chromatographic study of the changes in the endogenous Na+-K+-ATPase inhibitor during sodium loading in man]
DELVA, Pietro;
1984-01-01
Abstract
Semi-purified dog kidney Na+-K+-ATPase was cross-linked with ovalbumin. This immobilized enzyme was able to hydrolyse ATP and this hydrolysis was ouabain-sensitive. It was then used in batch wise affinity chromatography for the detection of endogenous Na+-K+-ATPase inhibitor in human plasma and urine. Ammonium acetate 1 mM washed off the endogenous Na+-K+-ATPase inhibitor from the immobilized enzyme. The inhibitory activity of the eluate from hypertensive plasma was significantly higher (p less than 0.0025, n = 6) than that of normotensive plasma. Similar results were obtained (n = 3) from human urine eluates during salt loading as compared to control urine.
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