论文部分内容阅读
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。
Hemoglobin (Gly-Hb 5%) in normal individuals, hemoglobin (Gly-Hb 10%) in patients with general diabetes, and hemoglobin in patients with severe diabetes (Gly-Hb 15%) were studied by Mossbauer method at liquid nitrogen temperature. The results show that there are three groups of electric quadrupole dipole interactions in the three hemoglobin samples, which respectively represent Oxy-Hb, Deoxy-Hb and Oxygen-free hemoglobin Low-spin hemoglobin (Ls-Hemo). In patients with hemoglobin in hemoglobin with oxygen significantly reduced the proportion of non-oxygenated hemoglobin components increased significantly. The experimental results also show that the hemoglobin does not contain trivalent Fe, but in oxygenated hemoglobin (Oxy-Hb) components, the experimental line width decreases with the increase of the proportion of glycosylation, indicating that Fe in normal human Oxyhemoglobin is not a single state, there are several similarities superimposed. The diabetic patients with the increasing severity of the oxygenated hemoglobin component of the experimental line width decreases while the Fe atom tends to a single state. This is an important phenomenon revealed by Mossbauer.