Haemoglobin(βK120C)-albumin trimer as an artificial O₂ carrier with sufficient haemoglobin allostery.

ABSTRACT: The allosteric O₂ release of haemoglobin (Hb) allows for efficient O₂ delivery from the lungs to the tissues. However, allostery is weakened in Hb-based O₂ carriers because the chemical modifications of the Lys- and Cys-β93 residues prevent the quaternary transition of Hb. In this paper, we describe the synthesis and O₂ binding properties of a recombinant Hb [rHb(βK120C)]-albumin heterotrimer that maintains sufficient Hb allostery. The rHb(βK120C) core, with two additional cysteine residues at the symmetrical positions on its protein surface, was expressed using yeast cells. The mutations did not influence either the O₂ binding characteristics or the quaternary transition of Hb. Maleimide-activated human serum albumins (HSAs) were coup

SUBMITTER: Morita Y 

PROVIDER: S-EPMC8341959 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature