Rahbar S, Nozari G, Ala F
Biochim Biophys Acta. 1979 Feb 26;576(2):466-70. doi: 10.1016/0005-2795(79)90421-5.
In a survey for abnormal haemoglobin variants in voluntary blood donors in Iran, a new variant was found in a young male who presented no clinical symptoms. It had the same electrophoretic mobility as haemoglobin D in alkaline buffers. Separation of the constituent polypeptide chains in acid urea buffer revealed it to be different from haemoglobin D previously found among Iranians. Analysis of its structure demonstrated a substitution to alanine (beta 47 Asp replaced by Ala) in the same residue as involved in haemoglobin G-Copenhagen (beta 47 Asp replaced by Asn).
在对伊朗自愿献血者进行的异常血红蛋白变体调查中，在一名无临床症状的年轻男性中发现了一种新变体。在碱性缓冲液中，它与血红蛋白D具有相同的电泳迁移率。在酸性尿素缓冲液中对组成多肽链进行分离后发现，它与之前在伊朗人当中发现的血红蛋白D不同。对其结构的分析表明，在与血红蛋白G-哥本哈根相同的残基处发生了丙氨酸替代（β47位天冬氨酸被丙氨酸替代）。
