Originals

Diabetologia

, Volume 38, Issue 9, pp 1076-1081

First online:

A new effective method for the evaluation of glycated intact plasma proteins in diabetic subjects

  • A. LapollaAffiliated withIstituto di Medicina Interna, Cattedra Malattie del Metabolismo, Università di Padova
  • , D. FedeleAffiliated withIstituto di Medicina Interna, Cattedra Malattie del Metabolismo, Università di Padova
  • , R. SeragliaAffiliated withArea di Ricerca CNR
  • , S. CatinellaAffiliated withArea di Ricerca CNR
  • , L. BaldoAffiliated withIstituto di Medicina Interna, Cattedra Malattie del Metabolismo, Università di Padova
  • , R. AronicaAffiliated withIstituto di Medicina Interna, Cattedra Malattie del Metabolismo, Università di Padova
  • , P. TraldiAffiliated withArea di Ricerca CNR

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Summary

The molecular weights of plasma proteins from healthy subjects and from patients with well-or badly-controlled diabetes mellitus have been determined by use of a matrix-assisted laser desorption ionization method, representing a highly accurate technique for the determination of the molecular weight of large biomolecules. Using this approach, different molecular weights of human serum albumin have been found for healthy (66,572–66,694 dalton) and diabetic (66,785–68,959 dalton) subjects. Such differences can be rationalized as being due to the different number of glucose molecules condensed on the protein and/or their further oxidation products; in the case of our diabetic patients this number is in the range of 1.4–14.8. The data show the high validity and specificity of the technique, which allows us to evaluate, without any protein degradation procedure, the number of glucose molecules condensed on a specific protein and ascertain the relationship of this number to the physiopathogenetic conditions of the subjects studied.

Key words

Protein glycation human serum albumin mass spectrometry laser desorption ionization