Baklouti F, Giraud Y, Francina A, Richard G, Favre-Gilly J, Delaunay J
CNRS UA 1171, Faculté de Médicine Grange-Blanche, Lyon, France.
Hemoglobin. 1988;12(2):171-7. doi: 10.3109/03630268808998023.
Hemoglobin Pierre-Bénite [beta 90(F6)Glu---Asp] is a new high affinity variant (P50 = 21.5 mm Hg), with normal heme-heme interaction, found in a French family. It was difficult to detect by conventional electrophoretic methods. However, the high performance liquid chromatography profile of its tryptic peptides contained an additional peak. Amino acid analysis of the corresponding peptide and determination of its sequence allowed us to identify the mutation. No instability was found. Mutations previously recorded in position 90 of the beta-chain display a positive charge shift and a reduced affinity for oxygen, whereas Hb Pierre-Bénite shows no charge shift and increased affinity for oxygen.
血红蛋白皮埃尔 - 贝尼泰[β90(F6)谷氨酸→天冬氨酸]是在一个法国家族中发现的一种新的高亲和力变体（P50 = 21.5毫米汞柱），具有正常的血红素 - 血红素相互作用。用传统电泳方法很难检测到它。然而，其胰蛋白酶肽段的高效液相色谱图谱中有一个额外的峰。对相应肽段进行氨基酸分析并确定其序列使我们能够鉴定出该突变。未发现不稳定性。先前记录在β链第90位的突变表现出正电荷转移和对氧的亲和力降低，而血红蛋白皮埃尔 - 贝尼泰没有电荷转移且对氧的亲和力增加。
