血红蛋白卢夫金：β29（B11）位的甘氨酸被天冬氨酸取代。一种涉及内部氨基酸残基的不稳定血红蛋白变体。

Hemoglobin Lufkin: beta 29 (B11) Gly replaced by Asp. An unstable hemoglobin variant involving an internal amino acid residue.

作者信息

Schmidt R M, Bechtel K C, Johnson M H, Therrell B L, Moo-Penn W F

出版信息

Hemoglobin. 1977;1(8):799-814. doi: 10.3109/03630267709003908.

Abstract

Hemoglobin Lufkin was found in a Black-American family. Structural analysis of the abnormal hemoglobin indicates a substitution of aspartic acid for glycine at position 29 in the beta chain. Marked instability of the variant hemoglobin is demonstrated by the rapid formation of inclusion bodies upon exposure of the red cells to redox dyes and by the large percentage of precipitated hemoglobin at 65 degrees C. The oxygen affinity, the Bohr effect, and the degree of cooperativity of Hb Lufkin and Hb A are similar over the physiologic pH range. However, at acid pH the oxygen affinity of the variant is increased. Unlike several other reported variants in the B helix, Hb Lufkin is not associated with methemoglobinemia.

摘要

血红蛋白卢夫金是在一个美籍非裔家庭中发现的。对这种异常血红蛋白的结构分析表明，β链第29位的甘氨酸被天冬氨酸替代。红细胞暴露于氧化还原染料后迅速形成包涵体，以及在65摄氏度时有很大比例的血红蛋白沉淀，都证明了这种变异血红蛋白具有明显的不稳定性。在生理pH范围内，血红蛋白卢夫金和血红蛋白A的氧亲和力、玻尔效应及协同程度相似。然而，在酸性pH条件下，该变异体的氧亲和力增加。与B螺旋中其他几个已报道的变异体不同，血红蛋白卢夫金与高铁血红蛋白血症无关。