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

Authors
  • Morita, Yoshitsugu1
  • Igarashi, Keisuke1
  • Funaki, Ryosuke1
  • Komatsu, Teruyuki1
  • 1 Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga Bunkyo-ku, Tokyo, 112-8551, Japan. , (Japan)
Type
Published Article
Journal
ChemBioChem
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jul 01, 2019
Volume
20
Issue
13
Pages
1684–1687
Identifiers
DOI: 10.1002/cbic.201900079
PMID: 30802345
Source
Medline
Keywords
Language
English
License
Unknown

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. © 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

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