A study of lipid effects on the digoxin immunoassay and on the binding to and activity of Na+/K+-ATPase.

The present study has examined the cross-reactivity of fatty acids and mono- and di-glycerides in the fluorescence polarization immunoassay for digoxin. The ability of these compounds to inhibit 86Rb uptake by the erythrocyte as well as their ability to displace 3H-ouabain from membrane-bound dog kidney ATP-ase was also assessed. Some unsaturated fatty acids (palmitoleic, palmitelaidic, oleic, linoleic, linolelaidic, linolenic, gamma-linolenic and arachidonic) were found to cross-react significantly in the digoxin immunoassay and to inhibit 3H-ouabain binding to membrane-bound Na+/K+-ATPase. Of the monoglycerides studied mono-11-eicosenoin was found to cross-react in the digoxin immunoassay, inhibit red cell 86Rb uptake and displace 3H-ouabain from its receptor, membrane-bound Na+/K+-ATPase. Two other monoglycerides, 1-monolinoleoyl and 1-monolinolenoyl glycerides, were able to displace 3H-ouabain from membrane-bound Na+/K+-ATPase, but had no effect on the digoxin immunoassay or on red cell 86Rb uptake.