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New fluorescence of nonenzymatically glucosylated human serum albumin

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
176
Issue
1
Identifiers
DOI: 10.1016/0014-5793(84)80905-9
Keywords
  • Nonenzymatic Glucosylation
  • Human Serum Albumin
  • Polylysine
  • Fluorescence
  • Energy Transfer
  • Aggregation
Disciplines
  • Physics

Abstract

Abstract Glucosylated human serum albumin (G-HSA) obtained under incubation with glucose at 37° C for 8 days showed a new fluorescence with a maximum at 430 nm, resulting in quenching of the fluorescence of only one tryptophan residue on HSA. The quantum yield of new fluorescence is 0.024 at 25° C. The analysis of the excitation spectra allowed us to conclude the absence of energy transfer. In G-HSA, non-disulfide cross-linking hexamer was confirmed by SDS-PAGE.

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