Duffy L K, Genaux C T, Stratton L P
Biochem Genet. 1976 Oct;14(9-10):809-21. doi: 10.1007/BF00485343.
The yellow-cheeked vole (Microtus xanthognathus) shows two electrophoretic hemoglobin components. Electrophoresis of the polypeptide chains from the separated hemoglobin components shows identical beta-chains but two alpha-chains of different mobility, alphaf and alphas. The composition of soluble tryptic peptides was determined for each alpha-chain. Amino acid differences were found in peptides alpha T1 and alpha T9; the compositions of the remainder of the homologous peptides were identical. Differences in alpha T1, found at alpha4 (alpha2-Gly-alphaf-Val) and alpha 5 (alphas-Thr-alphaf-Asp), were confirmed after a run to residue 20 of the fast component in an automatic sequencer. The differences in charge between alphaT1 peptides can account for the electrophoretic pattern of two hemoglobins. This is the first time that it has been possible to identity the residues which can account for the charge difference between the two hemoglobins observed in a Microtus species.
黄颊田鼠（Microtus xanthognathus）显示出两种电泳血红蛋白成分。对分离出的血红蛋白成分的多肽链进行电泳，结果显示β链相同，但有两条迁移率不同的α链，即αf和αs。测定了每条α链的可溶性胰蛋白酶肽的组成。在肽αT1和αT9中发现了氨基酸差异；其余同源肽的组成相同。在自动测序仪中对快速成分的第20个残基进行测序后，证实了αT1在α4（α2-甘氨酸-αf-缬氨酸）和α5（αs-苏氨酸-αf-天冬氨酸）处的差异。αT1肽之间的电荷差异可以解释两种血红蛋白的电泳图谱。这是首次能够鉴定出可解释在一种田鼠物种中观察到的两种血红蛋白之间电荷差异的残基。
