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

Chembiochem. 2019 Jul 1;20(13):1684-1687. doi: 10.1002/cbic.201900079. Epub 2019 May 17.

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.

Keywords: heme proteins; oxygen carriers; protein modifications; red blood cell substitutes; site-directed mutagenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / chemistry
  • Alanine / genetics
  • Amino Acid Substitution
  • Cysteine / genetics
  • Hemoglobins, Abnormal / genetics
  • Hemoglobins, Abnormal / metabolism*
  • Humans
  • Oxygen / metabolism*
  • Phytic Acid / metabolism*
  • Pichia / genetics
  • Protein Binding / genetics
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Serum Albumin, Human / metabolism*

Substances

  • Hemoglobins, Abnormal
  • Recombinant Proteins
  • Phytic Acid
  • Cysteine
  • Alanine
  • Oxygen
  • Serum Albumin, Human