Modification of Rat Hemopexin Properties upon Heme Binding

Rat hemopexin and its complex with heme were found to have the same Stokes' radius, 3.9 nm, as determined by gel filtration. Therefore no polymerisation occurs as a result of heme binding. The conformational parameters calculated from circular dichroism spectra indicate that hemopexin and its complex consist of 20%β sheet and mainly of disordered structure. No change of the secondary structure is therefore observed upon heme binding. Hemopexin reveals five bands by analytical electrofocusing with pI ranging from 5.5 to 5.95. This microheterogeneity is not due to sialic acid differences between the variants. Upon heme binding the pI of the variants decrease to lower values (from 4.8 to 5.25). This decrease in the pI value of hemopexin is thought to modify the tertiary structure through charge effects and may allow the binding of the heme‐hemopexin complex to the hepatocytes.