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Fig. 2 | Molecular Medicine

Fig. 2

From: Characterization of a Novel Hemoglobin-Glutathione Adduct That Is Elevated in Diabetic Patients

Fig. 2

Cation exchange and boronate affinity chromatography analyses of human diabetic hemoglobin. (A) Elution of hemoglobin peaks from a delipidated whole blood hemolysate obtained from a human diabetic patient and fractionated by cation exchange chromatography. Hemoglobin subfractions were assigned by identification of constituent globin chains as determined by subsequent HPLC and LCMS analyses. HbA0, hemoglobin with no modification to either the α- or β-chains; HbA1c, hemoglobin with an Amadori glycation product attached to the amino terminal valine of the globin β-chain; HbA1d3, hemoglobin modified by attachment of oxidized glutathione (HbASSG) as a mixed disulfide with the cysteine side chain at position 93 of the globin β-chain; Hb1e, hemoglobin with an Amadori glycation product attached to the amino terminal valine of the globin α-chain. (B) Fractionation of glycated hemoglobin fraction obtained by boronate affinity chromatography by ion exchange chromatography. glyc-HbA0, hemoglobin that is glycated at the lysine side chain of either the α- or β-chains (Al-Abed et al. unpublished data); HbA1c-SG, hemoglobin with a simultaneous Amadori glycation product and glutathionylation at cysteine side chain at position 93; glyc-HbA1d3, glycated hemoglobin that is also modified by attachment of glutathione (HbASSG) to the cysteine side chain at position 93 of the globin β-chain; HbA1e, hemoglobin with an Amadori glycation product attached to the amino terminal valine of the globin α-chain.

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