山羊血红蛋白的结构。V. 第四个β链变体（β-D-马耳他型；69位天冬氨酸被甘氨酸取代），氧亲和力降低，在马耳他以高频率出现。

The structure of goat hemoglobins. V. A fourth beta chain variant (beta-D-Malta; 69 Asp is replaced by Gly) with decreased oxygen affinity and occurring at a high frequency in Malta.

作者信息

Bannister J V, Bannister W H, Wilson J B, Lam H, Miller A, Huisman T H

出版信息

Hemoglobin. 1979;3(1):57-75. doi: 10.3109/03630267909069155.

Abstract

During a survey of hemoglobin types in goats in the Republic of Malta a variant (Goat Hb D-Malta) was discovered which differs from normal goat Hb A by the substitution of an aspartyl residue in position beta 69 (E13) by a glycyl residue. The gene frequency of the beta D allele was 0.255; 29 homozygous Hb D goats were present among 327 animals sampled. Homozygous Hb D goats also produce Hb C, whose beta chains are the product of a non-allelic beta C structural gene. Goat Hb D-Malta has a distinctly decreased affinity for molecular oxygen.

摘要

在对马耳他共和国山羊血红蛋白类型的调查中，发现了一种变体（山羊血红蛋白D - 马耳他型），它与正常山羊血红蛋白A的不同之处在于，β链69位（E13）的天冬氨酰残基被甘氨酰残基取代。βD等位基因的基因频率为0.255；在327只采样动物中有29只纯合血红蛋白D山羊。纯合血红蛋白D山羊还产生血红蛋白C，其β链是非等位βC结构基因的产物。山羊血红蛋白D - 马耳他型对分子氧的亲和力明显降低。