Schneider R G, Hettig R A, Bilunos M, Brimhall B
Hemoglobin. 1976;1(1):85-96. doi: 10.3109/03630267609031024.
The amino acid substitution in a new hemoglobin variant, Hb Baylor (alpha2beta281 (EF5) Leu replaced by Arg), has been determined by application of column chromatography and amino acid analysis of the tryptic peptides. The hemoglobin is somewhat unstable and it has a high oxygen affinity. The propositus shows the opposing hematologic effects of these two properties--the instability being associated with increased destruction, and the high O2 affinity with increased production, of erythrocytes.
一种新的血红蛋白变体Hb Baylor（α2β281（EF5）位点的亮氨酸被精氨酸取代）中的氨基酸替换，已通过柱色谱法和胰蛋白酶肽段的氨基酸分析得以确定。该血红蛋白有点不稳定，并且具有高氧亲和力。先证者表现出这两种特性相反的血液学效应——不稳定性与红细胞破坏增加相关，而高氧亲和力与红细胞生成增加相关。
