Nakatsuji T, Wilson J B, Huisman T H
Hemoglobin. 1984;8(1):37-46. doi: 10.3109/03630268408996959.
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.
科迪勒血红蛋白（Hb Cordele）在α链第47位（CE5）存在天冬氨酸被丙氨酸取代的情况，它是在居住于佐治亚州科迪勒的一对黑人双胞胎中发现的。通过对经高效液相色谱法分离得到的α链胰蛋白酶肽段进行分析，阐明了这种变体的结构。出生时，科迪勒血红蛋白约占总血红蛋白的21% - 23%，在其中一个婴儿3.5个月大时占30.4%。科迪勒血红蛋白具有正常的氧亲和力，但在60摄氏度时略有不稳定。已将其某些特性与小仓血红蛋白（Hb Kokura，α47天冬氨酸被甘氨酸取代）、哈沙龙血红蛋白（Hb Hasharon，α47天冬氨酸被组氨酸取代）和阿利亚血红蛋白（Hb Arya，α47天冬氨酸被天冬酰胺取代）的特性进行了比较。对科迪勒血红蛋白成年携带者的研究无法进行。
