The affinity glycated hemoglobin in a family with hereditary spherocytosis and in other non-hemoglobinopathic hemolytic anemias.

The glycated hemoglobin (GHb) is lowered by hemolytic anemia. The cation-exchange HbA1 has been shown to be lowered by hereditary spherocytosis (HS). The HbA1, however, can be increased by elevations of fetal hemoglobin (HbF). The affinity GHb, a parameter related to, but not identical with, the HbA1, and unaffected by HbF, has been shown to be low in hemoglobinopathies but not, to our knowledge, in HS and other non-hemoglobinopathic hemolytic anemias. Therefore, the affinity GHb and HbF was determined in four members of an HS family and in nine other cases of non-hemoglobinopathic hemolytic anemia, including three autoimmune hemolytic anemias, four red cell fragmentation syndromes (two "Waring blender" syndromes, one thrombotic thrombocytopenic purpura in association with tumor, and one case of disseminated intravascular coagulation), and two red cell membrane defects: paroxysmal nocturnal hemoglobinuria and another case of hereditary spherocytosis. The GHb for these nine cases was 3.6 +/- 1.7 percent (normal 6.0 +/- 2.0 percent; p less than 0.001). The reticulocyte count, available in four cases, was 0.23 +/- 0.14 and correlated negatively with the GHb. The average GHb in the HS family was 3.9 +/- 0.8 percent, which was significantly less than the normal of 6.0 +/- 2.0 percent (p less than 0.001); the HbF was less than 1.0 percent. It is concluded that the GHb is diminished in hemolytic anemias not associated with hemoglobinopathies and that this lowering reflects the shortened red cell life span in these processes. To our knowledge, this is the first report of low GHb in hemolytic anemia not associated with hemoglobinopathy, by the affinity chromatographic technique, as opposed to the cation-exchange chromatographic technique.