Add time:08/15/2019         Source:sciencedirect.com

The hydrolysis of β-(2-furyl)acryloyl phosphate (FAP), a synthetic substrate for the (Na+ + K+)-ATPase by the partially purified enzyme from rat brain and rat kidney, has been assessed. Using previously determined FAPase reaction conditions, it was discovered that the KI for ouabain of the α23 isozyme of the (Na+ + K+)-ATPase was ∼10−5 M, while for the α1 isozyme the KI was ∼10−3 M. These values were an order of magnitude higher (lower affinity) than the KI's for ouabain as determined when using ATP in a coupled assay for (Na+ + K+)-ATPase activity: ∼10−6 M and ∼10−4 M for the α23 and α1 isozymes, respectively. This discrepancy was alleviated by altering established reaction conditions. Previously published FAPase studies have overlooked this fact, since either the properties of the isozymes of the (Na+ + K+)-ATPase were unknown at that time, or ouabain titration profiles were never performed.

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