Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga Bunkyo-ku, Tokyo, 112-8551, Japan.
Chembiochem. 2019 Jul 1;20(13):1684-1687. doi: 10.1002/cbic.201900079. Epub 2019 May 17.
Covalent wrapping of recombinant human hemoglobin (Cys-β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)-HSA cluster as an artificial O carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O affinity moderately, in much the same way as that of naked hemoglobin. This reduction might be attributable to the inert, small Ala-β93 residue, which cannot be reacted with the bulky maleimide crosslinker.
通过人血清白蛋白（HSA）对重组人血红蛋白（Cys-β93→Ala）变体 rHb（βC93A）进行共价包裹，得到 rHb（βC93A）-HSA 复合物作为人工 O 载体作为红细胞替代品。六磷酸肌醇与中心 rHb（βC93A）核心的络合适度降低了 O 亲和力，与裸血红蛋白的方式非常相似。这种减少可能归因于惰性的、小的 Ala-β93 残基，它不能与大体积的马来酰亚胺交联剂反应。
