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

Authors :: Morita Y
Igarashi K
Funaki R
Komatsu T
Source :: Chembiochem : a European journal of chemical biology [Chembiochem] 2019 Jul 01; Vol. 20 (13), pp. 1684-1687. Date of Electronic Publication: 2019 May 17.
Publication Year :: 2019
Abstract: Covalent wrapping of recombinant human hemoglobin (Cys-β93→Ala) variant rHb(βC93A) by human serum albumin (HSA) yielded the rHb(βC93A)-HSA <subscript>3</subscript> cluster as an artificial O <subscript>2</subscript> carrier as a red blood cell substitute. Complexation of inositol hexaphosphate to the central rHb(βC93A) core reduced the O <subscript>2</subscript> 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.<br /> (© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)

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

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