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      High-performance liquid chromatographic assay of serum glycated albumin

      , , , , , , ,
      Diabetologia
      Springer Science and Business Media LLC

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          Fructosamine: A new approach to the estimation of serum glycosylprotein. An index of diabetic control

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            The principal site of nonenzymatic glycosylation of human serum albumin in vivo.

            We have determined the major site of nonenzymatic glycosylation of human serum albumin in vivo. This was accomplished by reacting freshly purified human serum albumin with sodium [3H]borohydride followed by aminoethylation and tryptic digestion. The tryptic peptides were separated into a soluble fraction which contained 88% of the total 3H radioactivity and an insoluble fraction. In order to isolate the 3H-labeled glycosylated peptides, the soluble tryptic peptide fraction was first subjected to boronic acid affinity chromatography. Cation exchange chromatography then separated the soluble glycosylated peptides into a major peak which contained 48% of the total recovered 3H radioactivity and a number of minor peptide fractions. The amino acid composition of the major peptide was: Thr, Glu2, Ala, Val2, Leu2, Lys, lysino-1-deoxysorbitol. In accord with the primary structure of human serum albumin, this amino acid composition corresponds precisely to residues 525-534. Glucitol-lysine, the NH2-terminal residue of this peptide, is totally resistant to cleavage by trypsin. Thus, lysine-525 is the predominant site of nonenzymatic glycosylation of human serum albumin in vivo. Chromatography on GlycoGel B boronic acid affinity gel indicates that 10-12% of normal serum albumin is glycosylated. The rate of nonenzymatic glycosylation of this protein in vivo is approximately 9 times that of human hemoglobin.
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              Enhanced nonenzymatic glucosylation of human serum albumin in diabetes mellitus.

              Use of an ion exchange chromatographic method and a colorimetric method with thiobarbituric acid showed that levels of nonenzymatically glucosylated serum albumin were increased in patients with poorly controlled diabetes mellitus compared to controls. The two methods correlated well (r = 0.99) and clearly discriminated between normal and poorly controlled diabetic populations. The levels of glycosylated hemoglobin were also measured in both populations. Several patients apparently in good control based on glycosylated hemoglobin measurements were found to have increased levels of glycosylated albumin. Because albumin has a shorter circulating half-life than does the human erythrocyte, the plasma concentration of glucosylated albumin should be expected to reflect short-term control of hyperglycemia in diabetes. The studies reported here suggest that the level of glucosylated albumin may indeed be a sensitive indicator of moderate hyperglycemia and of early glucose intolerance.
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                Author and article information

                Journal
                Diabetologia
                Diabetologia
                Springer Science and Business Media LLC
                0012-186X
                1432-0428
                August 1988
                August 1988
                : 31
                : 8
                : 627-631
                Article
                10.1007/BF00264772
                1a51976e-f56e-4068-b275-e8ef14dd8488
                © 1988

                http://www.springer.com/tdm

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