Plaseska D, de Alarcon P A, McMillan S, Walbrecht M, Wilson J B, Huisman T H
Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
Hemoglobin. 1990;14(4):423-9. doi: 10.3109/03630269009032002.
Hb Iowa with a Gly----Ala mutation at position beta 119(GH2) was observed in a Black infant and her mother. The baby was also heterozygous for Hb S; Hb Iowa was confused with Hb F at birth because its electrophoretic mobility was similar to that of Hb F1. The beta chain of Hb Iowa could be readily separated from the beta A, alpha, and gamma chains by polyacrylamide gel electrophoresis and by reversed phase high performance liquid chromatography. Structural characterization was through amino acid analyses of peptides isolated from a tryptic digest of the aminoethylated beta-Iowa chain. The Gly----Ala replacement in Hb Iowa does not affect its stability and oxygen carrying properties; hematological data for mother and child were within normal ranges.
在一名黑人婴儿及其母亲身上发现了位于β119（GH2）位置有甘氨酸→丙氨酸突变的爱荷华血红蛋白（Hb Iowa）。该婴儿也是镰状血红蛋白（Hb S）的杂合子；出生时爱荷华血红蛋白被误诊为胎儿血红蛋白（Hb F），因为其电泳迁移率与Hb F1相似。通过聚丙烯酰胺凝胶电泳和反相高效液相色谱法，爱荷华血红蛋白的β链可以很容易地与βA、α和γ链分离。通过对从氨乙基化的β - 爱荷华链胰蛋白酶消化物中分离出的肽段进行氨基酸分析来进行结构表征。爱荷华血红蛋白中甘氨酸→丙氨酸的替换并不影响其稳定性和携氧特性；母婴的血液学数据均在正常范围内。
