Hemoglobin(βC93A)–Albumin Cluster: Mutation of Cysteine‐β93 to Alanine Allows Moderate Reduction of O2 Affinity by Inositol Hexaphosphate. (17th May 2019)

• Record Type: Journal Article
• Authors: Morita, Yoshitsugu; Igarashi, Keisuke; Funaki, Ryosuke; Komatsu, Teruyuki
• Is Part Of: Chembiochem. Volume 20:Number 13(2019)
• Page Start: 1684
• Page End: 1687
• Publication Date: 2019-05-17
• Subjects: heme proteins -- oxygen carriers -- red blood cell substitutes -- protein modifications -- site-directed mutagenesis; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900079
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Covalent wrapping of recombinant human hemoglobin (Cys‐β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)‐HSA 3 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. Abstract : Accepting substitutes : A core–shell protein cluster comprising a recombinant human hemoglobin variant (rHb(βC93A)) at the center and human serum albumin (HSA) at the exterior is synthesized as an artificial O2 carrier to act as a substitute for red blood cells. The rHb(βC93A)‐HSA 3 cluster shows controllable O2 affinity by complexation of the allosteric effector inositol hexaphosphate.