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Hemoglobin
international journal for hemoglobin research
Volume 8, 1984 - Issue 1
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Original Article

HB Cordele α247(CE5)ASP→ALAβ2 A Mildly Unstable Variant Observed in Black Twins

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Pages 37-46 | Received 04 Aug 1983, Accepted 14 Sep 1983, Published online: 07 Jul 2009
 

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.

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