Identification of the carboxymethyllysine residue in the advanced stage of glycated human serum albumin

Article abstract of DOI:10.1248/cpb.40.705

As an advanced stage of glycation, glycated human serum albumin (G-HSA; glucose content, 2 mol of 5-hydroxymethylfurfural equivalent/mol of HSA) was incubated at 37°C up to 30 d in 0.2 M phosphate buffer, pH 7.4, with 100 μM Fe³⁺. G-HSA incubated for 30 d (G-HSA-30(Fe)) was subsequently hydrolyzed at 110 °C for 24 h in 6 N HCl. In the hydrolysate, N(ε)-carboxymethyllysine (CML) was identified by cochromatography with synthesized CML on an amino acid analyzer. pI of HSA (4.8) shifted to 4.5 in G-HSA. A more acidic fraction, pI 4.3, appeared in G-HSA-30(Fe). CML content (mol of CML/mol of HSA) of HSA and G-HSA was as follows; 0 in HSA, 0.2 in HSA-30(Fe), 0.4 in G-HSA and 1.5 in G-HSA-30(Fe) pI 4.3. The amino acid compositions also changed in lysine, arginine and tyrosine at the advanced stage of the reaction.

Full text of DOI:10.1248/cpb.40.705

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