Polymerization of Hemoglobins of Mouse and Man: Structural Basis

Abstract

Human hemoglobin Pôrto Alegre and mouse hemoglobin (BALB/cJ) polymerize by forming intermolecular disulfide bridges. Both hemoglobins have externally oriented, reactive cysteinyl residues in the A-helix of the beta chain. Hemoglobin Pôrto Alegre can be designated as α₂ β₂^{9 Ser → Cys}. The crysteinyl residue of the mouse hemoglobin is at position 13 in the beta chain.