Title : Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.

Pub. Date : 2004 Jun 25

PMID : 15102834






2 Functional Relationships(s)
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1 The radiolabeled peptides containing reduced fructosamine 3-phosphates bound to Lys-alpha-16, Lys-alpha-139, and Lys-beta-17 were much less abundant if the hemoglobin substrate used for the in vitro phosphorylation with FN3K and [gamma-(32)P]ATP came from erythrocytes incubated with an elevated glucose concentration in the absence of DMF, indicating that these lysine residues had been substantially deglycated in intact cells when FN3K action was unrefrained. fructosamine 3-phosphates fructosamine 3 kinase Homo sapiens
2 The radiolabeled peptides containing reduced fructosamine 3-phosphates bound to Lys-alpha-16, Lys-alpha-139, and Lys-beta-17 were much less abundant if the hemoglobin substrate used for the in vitro phosphorylation with FN3K and [gamma-(32)P]ATP came from erythrocytes incubated with an elevated glucose concentration in the absence of DMF, indicating that these lysine residues had been substantially deglycated in intact cells when FN3K action was unrefrained. fructosamine 3-phosphates fructosamine 3 kinase Homo sapiens