Study of Hemoglobin and Human Serum Albumin Glycation with Electrochemical Techniques |
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Authors: | Jinghua Yang Jing Zhao Han Xiao Dongmei Zhang Genxi Li |
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Institution: | 1. Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, P.?R. China tel: +86?25?83593596;2. fax: +86?25?83592510;3. Laboratory of Biosensing Technology, School of Life Science, Shanghai University, Shanghai 200444, P.?R. China |
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Abstract: | 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 O2 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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Keywords: | Hemoglobin Human serum albumin Heme Nonenzymatic glycation Diabetes mellitus |
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