Nakatsuji T, Lam H, Wilson J B, Webber B B, Huisman T H
Hemoglobin. 1982;6(6):593-8. doi: 10.3109/03630268209046452.
A new gamma chain variant with an electrophoretic mobility at pH 8.1 between those of Hb S and Hb C was isolated and quantitated by DEAE-cellulose chromatography. It was readily identified with the use of various micro-chromatographic and sequencing procedures as alpha 2 G gamma 2 94(FGl)Asp replaced by Asn. The hemoglobin was named Hb F-Columbus-Ga. The quantity of this G gamma chain variant (as % total gamma chain) was about 39% and the percentages of the normal G gamma and A gamma I chains were 37% and 24%, respectively.
通过DEAE - 纤维素色谱法分离并定量了一种新的γ链变体,其在pH 8.1时的电泳迁移率介于Hb S和Hb C之间。使用各种微色谱和测序方法很容易鉴定出它是α2Gγ2 94(FGl)Asp被Asn取代。该血红蛋白被命名为Hb F - Columbus - Ga。这种Gγ链变体的量(占总γ链的百分比)约为39%,正常Gγ链和AγI链的百分比分别为37%和24%。