在大肠杆菌中合成的β(NA1)Val缺失、(NA2)His→Met血红蛋白的功能特性。
Functional properties of beta(NA1)Val-deleted,(NA2)His-->Met hemoglobin synthesized in Escherichia coli.
作者信息
Baudin V, Bihoreau M T, Kister J, Marden M, Pagnier J, Poyart C
机构信息
INSERM U299 Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.
出版信息
Artif Cells Blood Substit Immobil Biotechnol. 1994;22(3):739-45. doi: 10.3109/10731199409117906.
Bovine Hb (hemoglobin) has a low oxygen affinity in the absence of chloride ions and DPG. Because of the increasing interest of this Hb as a potential blood substitute we have engineered a human Hb mutant with the aim of mimicking the functional properties of bovine Hb. This was achieved by deleting residue beta NA1 Val and substituting a methionine for histidine at the beta NA2 position as previously suggested by Perutz and Imai in 1980. Our results show that the artificial mutant exhibits some of the characteristics of bovine Hb but does not show the low oxygen affinity which is measured in bovine blood.
在没有氯离子和二磷酸甘油酸（DPG）的情况下，牛血红蛋白（Hb）对氧气的亲和力较低。由于人们对这种血红蛋白作为潜在血液替代品的兴趣日益浓厚，我们设计了一种人血红蛋白突变体，旨在模拟牛血红蛋白的功能特性。这是通过删除β链NA1位的缬氨酸残基，并按照佩鲁茨和今井在1980年之前所建议的，在β链NA2位用甲硫氨酸取代组氨酸来实现的。我们的结果表明，这种人工突变体表现出了一些牛血红蛋白的特征，但并未表现出在牛血液中测得的低氧亲和力。
Zotero 插件