166903-94-2Relevant academic research and scientific papers
Systematically cross-linked human hemoglobin: Functional effects of 10 ? spans between beta subunits at lysine-82
Kluger, Ronald,Shen, Lixin,Xiao, Hong,Jones, Richard T.
, p. 8782 - 8786 (1996)
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 ? cross-link between the ε-amino groups of each β-lys-82 of human hemoglobin. The oxygen affinity of the modified proteins fits the correlation interpolated from those for shorter and longer cross-links. The oxygen binding curve shows a high degree of cooperativity. These results support the idea that the length of the semirigid cross-link in a structurally homogeneous series constrains the relaxation of the protein upon oxygen binding by a mechanism that is specifically reflected in the oxygen affinity, while interactions between hemes that affect cooperativity are not diminished.
