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Reaction of Human CO Hemoglobin with p,p'-Difluoro-m,m'-dinitrodiphenylsulfone

From the ¹ From the Department of Biochemistry, University of Tennessee Medical Units, Memphis, Tennessee 38103

The reaction of human CO hemoglobin with p,p'-difluorom,m'-dinitrodiphenylsulfone was shown to result in the formation of an intramolecular cross-link between the amino-terminal valine residues of the chains. The cross-linked hemoglobin was isolated by gel filtration in 1 m MgCl₂ and ion exchange chromatography. Oxygen dissociation studies on the purified cross-linked hemoglobin revealed that it had a high oxygen affnity (P₅₀ = 0.82 mm) and exhibited no heme-heme interactions.

Although the major reaction product was the species cross-linked between the amino-terminal residues of the chain, it was shown that cross-links between ß dimers were also formed at other, as yet unidentified, locations.

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