Interference by fast hemoglobin variants in the column-chromatographic assay for glycosylated hemoglobin.

The anode Is at the left, the origin at the rlt. Above Is a control consIstIng of HbA, F. S. and A2.Below Is the concentrated column eluate. Note the fast hemoglobIn band at the far left and carbonIc anhy-&ase B near the origIn atthe rIght In the pattern for the column eluate 1250 CLINICAL CHEMISTRY. dure is applicable also to other situations , e.g.,to the measurements of specific radioactivity in which the mass is determined by radioimmunoassay (3). In some measurements of this kind, as for instance in the test of validity (4,5), widely different amounts of radioactive material are present in radioimmu-noasay tubes. This makes the above correction indispensable. action law with antibody heterogeneity. Exact correction for variable mass of labeled ligand. method to assess radiochemical purity of compounds measured by radioimmunoassay. of radioimmunoassay validity in the presence of an isotope effect. Recently we reported a normal column -chromatographic glycosylated hemoglobin in the presence of a fast hemoglobin variant (putative HbN-Baltimore) (1). Since submission of that manuscript we have learned that another fast hemoglobin, HbH, can increase concentrations of glycosylated hemoglobin (2). Therefore, we undertook further chromatographic and electrophoretic studies of the glycosyl-ation of our fast hemoglobin variant to resolve this apparent conflict. Our patient's hemolysate was subjected to ion-exchange chromatography for glycosylated hemoglobin de