[Affinity chromatographic study of the changes in the endogenous Na+-K+-ATPase inhibitor during sodium loading in man].
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.
D000818:Animals; D002846:Chromatography, Affinity; D004285:Dogs; D004800:Enzymes, Immobilized; D006801:Humans; D006973:Hypertension / Q000201:enzymology; D010042:Ouabain / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors*
D004800:Enzymes, Immobilized; D010042:Ouabain; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase
Etude par chromatographie d'affinité de la variation chez l'homme pendant une surcharge sodée de l'inhibiteur endogène de la Na+-K+-ATPase.