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Diabetes and Protein Glycosylation pp 17–41Cite as

Measurement

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Abstract

Early techniques for the separation of minor hemoglobin components utilized starch block electrophoresis and carboxymethylcellulose chromatography. 1,2 These techniques not only provided means for separation on minor components, but were also instrumental in their identification and in the development of a system of nomenclature. Ion-exchange chromatography remains one of the most commonly employed methods for separation of minor hemoglobin fractions from hemoglobin A, but the original tedious techniques have been replaced in most clinical chemistry laboratories by commercially available minicolumn systems that are marketed as kits complete with prepacked columns, prepared buffers, and lyophilized standards.3–6 Affinity chromatography on phenylboronate, also commercially marketed as minicolumns in prepackaged kits, have become popular for measurement of glycosylated hemoglobin.7–14 Another simple and widely employed technique entails measurement of the colored product after reaction with thiobarbituric acid (TBA)15–21; fluorometric detection of formaldehyde released after periodate oxidation of hemoglobin-linked carbohydrate groups is an alternative method.22

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  1. Division of Endocrinology and Metabolism, University of Medicine and Denstistry of New Jersey, 07103, Newark, New Jersey, USA

    Margo Panush Cohen (Professor of Medicine and Chair)

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Cohen, M.P. (1986). Measurement. In: Diabetes and Protein Glycosylation. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4938-2_3

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