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PubMed1990

Determination of cardiac glycosides in digitoxin tablets and deslanoside injections by micro-HPLC.

A micro high-performance liquid chromatographic (micro-HPLC) procedure for the assay of digitoxin tablets and deslanoside injections has been developed. Micro-HPLC is performed on an ODS micro column, with acetonitrile-methanol-water (10:20:17) for digitoxin tablets and acetonitrile-water (21:70) for deslanoside injections. The effluent is monitored by UV absorption at 220 nm. Quantitation of cardiac glycosides in tablets and injections is carried out by the internal standard method. The composite assay results for digitoxin tablets and deslanoside injections provide average values of 101.2 and 99.9% with standard deviations of 1.2 and 0.93%, respectively. This micro-HPLC method is sensitive, quantitative, and reproducible. It is suitable for use in examining the content uniformity of pharmaceutical preparations.

Chromatography, High Pressure Liquid↗
PubMed1997

Fluoresceinyl-ethylenediamine-ouabain detects an acidic environment in the cardiac glycoside binding site of Na+/K+-ATPase.

To probe the pH value in the microenvironment of the cardiac glycoside-binding site of Na+/K+-ATPase, pH-sensitive fluorescent derivatives of ouabain were synthesized. The fluoresceinyl derivative of ethylenediamino-ouabain (FEDO) had a pKs of 6.0 and showed a H+-dependent fluorescence change, when its ratio of excitation at 490 nm/450 nm was recorded at 530 nm. Binding of FEDO inactivated Na+/K+-ATPase at 37 degrees C and pH 7.25 in a slow time-dependent process under the conditions of backdoor phosphorylation with k(on) of 891 s(-1) M(-1). The complex dissociated with k(on) of 0.35 x 10(-3) s(-1) resulting in a Kd value of 0.4 microM for the FEDO x enzyme complex. Binding of FEDO was associated with a decrease of the excitatory fluorescence ratio at 490 nm/450 nm which could be used to convert this change into a pH value. A pH value of 5.1 +/- 0.2 was calculated to exist in the microenvironment of the FEDO x enzyme complex. This pH value was independent of the pH of the incubation medium used to form the FEDO x enzyme complex. Analysis of the accessibility of the fluorophore in the FEDO x enzyme complex to the dynamic quencher potassium iodide detected a decrease of the Stern-Volmer constant from 6.2 mM(-1) (free FEDO) to 1.5 mM(-1) (FEDO x enzyme complex) indicating thereby a limited accessibility of the fluorophore to anions. Analysis of the microenvironment of the fluorescein residue of the FEDO x enzyme complex by measurements of the anisotropy and the fluorescence half-life time revealed that both processes differed significantly when H2O was replaced by D2O. We conclude, therefore, that a pH of 5.1 +/- 0.2 exists in the vicinity of ouabain that is hidden in the depth of the receptor site when the ouabain receptor complex has been formed.

Animals↗