Immobilized human hemoglobin, a versatile matrix for analytical and biotechnological applications.
The analytical and biotechnological applications of human hemoglobin immobilized covalently on CNBr-Sepharose 4B are reviewed. Hemoglobin is bound to the matrix as alphabeta dimers via either chain. The immobilized alphabeta dimers maintain the capacity to interact reversibly with soluble ones under conditions where the soluble protein is in self-association equilibrium. Under these conditions, therefore, immobilized dimers bind part of the soluble protein. In turn, the binding process can be used to assess the specific features of the equilibrium on solid-phase and to extract selectively hemoglobin from a variety of biological specimens of practical interest. A different application of immobilized alphabeta dimers concerns their use in the determination of the equilibrium and kinetic stability of the heme-globin linkage, a property that is directly correlated with the stability of the hemoglobin molecule. The advantages and limitations attendant the use of the immobilized protein relative to the soluble one are discussed.
Chiancone
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CNR Center of Molecular Biology, Department of Biochemical Sciences A. Rossi Fanelli, University La Sapienza, Rome, Italy.
Gattoni
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Boffi
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D001709:Biotechnology / Q000379:methods*; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D019281:Dimerization; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans
D006454:Hemoglobins