Hemoglobin(βC93A)-Albumin Cluster: Mutation of Cysteine-β93 to Alanine Allows Moderate Reduction of O2 Affinity by Inositol Hexaphosphate

Chembiochem : a European Journal of Chemical Biology
Yoshitsugu MoritaTeruyuki Komatsu

Abstract

Covalent wrapping of recombinant human hemoglobin (Cys-β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)-HSA3 cluster as an artificial O2 carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O2 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.

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Jul 30, 2015·Scientific Reports·Risa HarukiTeruyuki Komatsu
Nov 18, 2018·The Journal of Physical Chemistry. B·Yoshitsugu MoritaTeruyuki Komatsu
Aug 14, 2015·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Takuya KimuraTeruyuki Komatsu

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Citations

Dec 17, 2019·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Ryosuke FunakiTeruyuki Komatsu
Aug 31, 2021·RSC Chemical Biology·Yoshitsugu MoritaTeruyuki Komatsu
Sep 10, 2021·Chemical Communications : Chem Comm·Yoshitsugu MoritaTeruyuki Komatsu

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