Related Experiment Videos
Hb Cordele alpha(2)47 (CE5)Asp----Ala beta 2. A mildly unstable variant observed in black twins
Hemoglobin
|January 1, 1984
Abstract:
Hb Cordele, which has an Asp----Ala substitution at position 47 (CE5) of the alpha chain, was discovered in Black twins living in Cordele, Georgia. The structure of this variant was elucidated through analyses of tryptic peptides of the alpha 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 degrees C. Some of its properties have been compared with those of Hb Kokura (alpha 47 Asp----Gly), Hb Hasharon (alpha 47 Asp----His), and Hb Arya (alpha 47 Asp----Asn). Studies on an adult carrier of Hb Cordele were not possible.