Haptoglobin: Retrospectives and Perspectives

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Abstract
Plasma haptoglobin is a genetically determined α2-acidic glycoprotein which combines specifically with hemoglobin, showing an activity of the “true” peroxidase type (for a review, see Reference 1). The binding of haptoglobin to hemoglobin is one of the strongest known noncovalent interactions in biology, the association constant being greater than 10−15 M. 2 Hemoglobin that has been released into the bloodstream by red cell hemolysis is effectively bound by haptoglobin. This mechanism prevents passage of hemoglobin through the glomerules and/or its deposition in the renal tubules; hence, iron remains available for further metabolic use. However, the complex is catabolized in the reticuloendothelial system in the liver; thus, haptoglobin cannot be considered as a regular transport protein (e.g., transferrin for iron, hemopexin for heme, etc.), but is regarded as a suicidal one.

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