Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

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Abstract

The sequential changes that occur during the precipitation on mild heating of the unstable hemoglobins, Hb Christchurch, Hb Sydney, Hb Köln, and Hb A, were examined with particular attention to the possibility of an accompanying oxidative process. Hb Christchurch, Hb Sydney, and Hb A precipitated with equal amounts of α- and β-chains and full heme complement. Hb Köln, however, was one-half hemedepleted and showed a slight excess of precipitated β-chains. In all cases the spectrum of the precipitated material was typical of a hemichrome. There was no evidence that sulfhydryl oxidation contributed to the precipitation process. Reduced glutathione was unable to protect the hemoglobin against precipitation, and mixed disulfide formation between the precipitating hemoglobin and glutathione was insignificant, even in the presence of excess glutathione. No blockade of β93 cysteines could be demonstrated in the unstable hemoglobins.

Authors

Christine C. Winterbourn, R. W. Carrell