Study of Hemoglobin and Human Serum Albumin Glycation with Electrochemical Techniques

被引：15
作者：
Yang, Jinghua [1 ,2 ]
Zhao, Jing [1 ,2 ]
Xiao, Han [1 ,2 ]
Zhang, Dongmei [1 ,2 ]
Li, Genxi [1 ,2 ,3 ]
机构：
[1] Nanjing Univ, Dept Biochem, Nanjing 210093, Peoples R China
[2] Nanjing Univ, Natl Key Lab Pharmaceut Biotechnol, Nanjing 210093, Peoples R China
[3] Shanghai Univ, Sch Life Sci, Lab Biosensing Technol, Shanghai 200444, Peoples R China
来源：
ELECTROANALYSIS | 2011年 / 23卷 / 02期
基金：
中国国家自然科学基金;
关键词：
Hemoglobin; Human serum albumin; Heme; Nonenzymatic glycation; Diabetes mellitus; ELECTRON-TRANSFER REACTIVITY; TYPE-2; DIABETES-MELLITUS; NONENZYMATIC GLYCATION; ALLOSTERIC MODULATION; BINDING; PROTEIN; MYOGLOBIN; FILMS; DRUG;
D O I：
10.1002/elan.201000193
中图分类号：
O65 [分析化学];
学科分类号：
070302 ; 081704 ;
摘要：
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.
引用
收藏
页码：463 / 468
页数：6
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