Suppr超能文献

用穆斯堡尔谱对两种脱氧血红蛋白-触珠蛋白复合物进行的研究。

Investigation of two deoxygenated haemoglobin-haptoglobin complexes by Mössbauer spectroscopy.

作者信息

Alfsen A, Bade D, Bürck U, Eicher H, Formanek S, Kalvius G M, Lavialle F, Mayer A, Parak F, Tejada J, Thomanek U F

出版信息

Biophys Struct Mech. 1977 Sep 28;3(3-4):229-38. doi: 10.1007/BF00535698.

Abstract

Haemoglobin Haptoglobin complexes formed when [Hp+]/[Hb]= 1/1 and [Hp]/[Hb] =2/1 were investigated by 57Fe Mössbauer spectroscopy. Both samples gave a spectrum consisting of a single quadrupole doublet. The temperature dependence of the quadrupole splitting was also identical for both samples. This proves that in both samples the nearest neighbour environment of the iron atom must be the same. A comparison with earlier investigations on myoglobin and haemoglobin indicates that the electronic structure of iron in the HbHp-complexes is similar to that in myoglobin.

摘要

通过57Fe穆斯堡尔光谱研究了当[Hp+]/[Hb]=1/1和[Hp]/[Hb]=2/1时形成的血红蛋白-触珠蛋白复合物。两个样品都给出了由单个四极双峰组成的光谱。两个样品的四极分裂的温度依赖性也相同。这证明在两个样品中,铁原子的最近邻环境一定是相同的。与早期对肌红蛋白和血红蛋白的研究比较表明,血红蛋白-触珠蛋白复合物中铁的电子结构与肌红蛋白中的相似。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验