Determination of Theophylline Binding to Human Serum Proteins by Isotachophoresis

J.C. Reijenga, A.P.M. Gaijkema, F.E.P. Mikkers

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Free theophylline was isolated from human serum by ultrafiltration and analysed in a leading electrolyte of 7.5 mM morpholinoethanesulphoric acid with ammediol as a counter ion at pH 8.90 and -alanine as a terminator. The UV (280 nm) absorbance of the theophylline spike between serine and bicine as spacers was integrated. Binding percentages to human pool serum, human albumin and 1-acid glycoprotein (orosomucoid) were determined at physiological concentrations, and found to be 55, 44 and 12%, respectively. The calibration lines were straight from 0 to 30 mg/l, with a standard deviation of 0.2 mg/l. The detection limit was 1 mg/l. The time of analysis was 12 min at 40 A in a 0.2 mm I.D. capillary.
Original languageEnglish
Pages (from-to)365-370
JournalJournal of Chromatography
Issue number1
Publication statusPublished - 1984


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