Abstract
A fast-moving abnormal hemoglobin found in a diabetic patient was identified as β140 (H18) ALA→ASP. It comprised about 40 % of the total hemoglobin. The β-terminal glycation in the abnormal hemoglobin was estimated to be 3 times as much as that in Hb A in the same blood sample. The abnormal hemoglobin was slightly unstable. Oxygen affinity of the stripped hemoglobin was decreased, but that of red cells from the carrier was slightly higher than normal because of the reduced effect of 2,3-diphosphoglycerate.