Hemoglobin(βC93A)-Albumin Cluster: Mutation of Cysteine-β93 to Alanine Allows Moderate Reduction of O 2 Affinity by Inositol Hexaphosphate

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 m...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2019-07, Vol.20 (13), p.1684-1687
Main Authors: Morita, Yoshitsugu, Igarashi, Keisuke, Funaki, Ryosuke, Komatsu, Teruyuki
Format: Article
Language:English
Subjects:
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
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Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201900079