Journal
ELECTROANALYSIS
Volume 23, Issue 2, Pages 463-468Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/elan.201000193
Keywords
Hemoglobin; Human serum albumin; Heme; Nonenzymatic glycation; Diabetes mellitus
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Funding
- National Natural Science Foundation of China [20575028]
- Natural Science Foundation of Jiangsu Province [BK2008268]
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High concentration glucose in diabetes mellitus may stimulate nonenzymatic glycation of proteins. Hemoglobin (Hb) and human serum albumin (HSA) are among the most sensitive proteins for the modification by glucose. In this paper, we report our study of Hb and HSA modification by glucose using electrochemical methods. Compared with native Hb, it is found that highly glycated Hb presents lower electron transfer reactivity and electrocatalytic activity toward O-2 and H2O2, and the glycation is glucose concentration and time dependent. Meanwhile, the changes of the electrochemical signal of heme after binding with HSA and glycated HSA have also suggested that proteins modified by high concentration glucose lasting for months and years in diabetes mellitus might be the reason for diabetes mellitus complication.
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