The structure and properties of hemoglobin are altered by the introduction of cross-links of defined structure between specific residues. The bis methyl phosphates and bis 3, 5- dibromosalicylates of 4-carboxy-trans-cinnamic acid as well as the bis methyl phosphate of 2, 6-naphthalenedicarboxylic acid produce a 10 Å cross-link between the ε-amino groups of each β-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the ...
