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Membrane-immobilized haptoglobin as affinity matrix for a hemoglobin-A1c immunosensor by Daniela Stöllner; Walter Stöcklein; Frieder Scheller; Axel Warsinke is a Chemistry article available to read on EtoBox.

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An amperometric immunosensor for hemoglobin-A1c (HbA1c) determination has been developed utilizing membraneimmobilized haptoglobin as affinity matrix fixed in front of a Pt-working electrode. The HbA1c assay was carried out in a two-step procedure including the selective hemoglobin enrichment on the sensor surface and the specific HbA1c detection by a glucose oxidase (GOx) labeled anti-HbA1c antibody. Hydrogen peroxide generated by the enzyme label was oxidized at +600 mV versus Ag/AgCl. A standard curve for HbA1c was obtained with a linear range between 0 and 25% HbA1c of total hemoglobin which correspond to 7.8-39 nM. ELISA studies confirmed the advantage of a sandwich-type format with haptoglobin as capture molecule for selective hemoglobin binding over the direct adsorption method. Results by the sandwich immunoassay showed a linear correlation within the clinically relevant range 5-20% (CV < 3). For sensor application the immobilization procedure of haptoglobin onto CDI-activated cellulose membranes was optimized.

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Author

Daniela Stöllner; Walter Stöcklein; Frieder Scheller; Axel Warsinke

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0003-2670)

Published

2002

Language

EN

Field

Chemistry (Physical Sciences)