摘要
对正常人的血红蛋白（Ｇｌｙ－Ｈｂ５％）、一般糖尿病患者的血红蛋白（Ｇｌｙ－Ｈｂ１０％）和严重糖尿病患者的血红蛋白（Ｇｌｙ－Ｈｂ１５％）用穆斯堡尔方法在液氮温度进行了研究。结果表明，在上述３种血红蛋白的样品中都存在三组双线劈裂的电四极相互作用，其分别表示带氧的血红蛋白（Ｏｘｙ－Ｈｂ）、不带氧的血红蛋白（Ｄｅｏｘｙ－Ｈｂ）及低自旋的血色素（Ｌｓ－Ｈｅｍｏ）。在糖尿病患者的血红蛋白中带氧的血红蛋白组分明显减少而不带氧的血红蛋白组分明显增加。实验结果还表明，在血红蛋白中不含三价Ｆｅ，但在带氧的血红蛋白（Ｏｘｙ－Ｈｂ）组分中，其实验线宽度随糖基化比重增加而不断减小，说明Ｆｅ在正常人的带氧血红蛋白中并非单一态，是有几个相似态叠加而成。而糖尿病患者随病情的不断加剧，其带氧血红蛋白组分中的实验线宽度不断减小而Ｆｅ原子趋向单一态。这是穆斯堡尔谱能揭示的一个重要现象。
The hemoglobins from normal adults (Gly-Hb 5%), people infected with diabetes (Gly-Hb 10%) and serious diabetics (Gly-Hb 15%) were investigated by Mossbauer spectyoscopy at liquid nitrogen temperature. All the experimental spectra of hemoglobin are composed of three doublets corresponding to oxy-hemoglobin (Oxy-Hb), deoxy-hemoglobin (Deoxy-Hb) and low-spin hemochrome (Ls-Hemo) respectively. It is found that Oxy-Hb is decreasing but Deoxy-Hb increasing for diabetes. Experimental results also indicate that the line-width of Mossbauer spectra of Oxy-Hb for diabetics is narrower than that for normal adults, showing that while Fe in Oxy-Hb exists in pile-up of some similar states for normal adults, bat it becomes in single state for serious diabetes.
出处
《核技术》
EI
CAS
CSCD
北大核心
2000年第2期83-85,共3页
Nuclear Techniques
