A study on the structures of hemoglobin of diabetic   patients by EXAFS technique

WANG Yinsong  1  WU Zhonghua  2  GE Yongxin  3  ZHANG Hongde  3    TAN Mingguang  1  ZHANG Guilin  1  1

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A study on the structures of hemoglobin of diabetic patients by EXAFS technique

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- A study on the structures of hemoglobin of diabetic patients by EXAFS technique
- NUCLEAR TECHNIQUES Issue 6, (2001)
- 作者机构：
  
  1. 中国科学院上海原子核研究所,上海,201800
  2. 中国科学院高能物理研究所,北京,100039
  3. 上海市第一人民医院,上海,200080
- 作者简介：
- 基金信息：
  
  中国科学院”九五”重大项目科学基金! (No .KJ95 1-A1- 40 9)
- DOI：
  CLC： R587.1
- Published：01 June 2001
- 稿件说明：
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[1]王荫淞,吴忠华,葛永新,张洪德,谈明光,张桂林.用EXAFS法研究糖尿病人血红蛋白的结构[J].核技术,2001(06):483-486.

WANG Yinsong 1 WU Zhonghua 2 GE Yongxin 3 ZHANG Hongde 3 TAN Mingguang 1 ZHANG Guilin 1 1. A study on the structures of hemoglobin of diabetic patients by EXAFS technique[J]. Nuclear techniques, 2001, (6): 483-486.
[1]王荫淞,吴忠华,葛永新,张洪德,谈明光,张桂林.用EXAFS法研究糖尿病人血红蛋白的结构[J].核技术,2001(06):483-486. DOI：

WANG Yinsong 1 WU Zhonghua 2 GE Yongxin 3 ZHANG Hongde 3 TAN Mingguang 1 ZHANG Guilin 1 1. A study on the structures of hemoglobin of diabetic patients by EXAFS technique[J]. Nuclear techniques, 2001, (6): 483-486. DOI：

摘要

血红蛋白是血液循环中输送氧的载体。糖尿病病人的血液中糖基化血红蛋白含量增加

影响了输氧的能力。我们用EXAFS法测定了正常人、轻度糖尿病病人以及重度糖尿病病人血红蛋白中铁原子的近邻结构。观察了糖尿病与血红蛋白结构的关系。结果表明

3种样品中铁原子的配位数和Fe—O键长基本相同

但重度糖尿病病人样品的Fe—N键长增加了 0 .0 0 2nm。这可能是由于他们的血液中脱氧血红蛋白的含量增加所引起

Abstract

Hemoglobin was the carrier of oxygen in blood circulation. For the patients with diabetes mellitus the enhencement of glycated hemoglobin in blood causes the decrease of oxygen transmission function. In this work

the local atomic structures of iron in hemoglobin were determined by EXAFS techniques. The relationship between diabetes mellitus and hemoglobin structures was observed. The blood samples were taken from normal people

slight and serious diabetic patients. The results show that the coordination number of iron atoms and Fe—O bond length were almost the same for the three samples. However

for the samples of serious diabetic patients the Fe—N bond length increases by about 0.002nm

the possible reasons were the increase of deoxyhemoglobin contents in their blood.

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