Abstract
Hb Cordele, which has an Asp→Ala substitution at position 47 (CE5) of the a chain, was discovered in Black twins living in Cordele, Georgia. The structure of this variant was elucidated through analyses of tryptic peptides of the a chain which were isolated by high performance liquid chromatography. At birth, Hb Cordele accounted for about 21-23% of total hemoglobin, and for 30.4% in one of the babies at age 3.5 months. Hb Cordele has a normal oxygen affinity, but is mildly unstable at 60°C. Some of its properties have been compared with those of Hb Kokura (α47 Asp→Gly), Hb Hasharon (α47 Asp→His), and Hb Arya (α47 Aspdsn). Studies on an adult carrier of Hb Cordele were not possible.