一例β55Met·O血红蛋白的结构分析

Structural Analysis of a Hemoglobin with β 55 Met Sulfoxide

将山东省招远市一慢电泳异常血红蛋白（ Ｈｂ）先证者血及正常人血分离纯化出珠蛋白，脲处理解链，再层析分离并纯化出正常及异常 β链．经胰蛋白酶水解，所得肽片段用 Ｈ Ｐ Ｌ Ｃ 分出酶解物中异常肽，此肽经氨基酸组成及顺序测定，表明它同于正常 β链的十九肽 β４１→５９；异常肽不被 Ｃ Ｎ Ｂｒ 作用，将它与正常十九肽通过质谱仪测定质荷比．结果说明异常肽的 β５５ Ｍ ｅｔ转变为亚砜型的 β５５ Ｍ ｅｔ· Ｏ，这转变是此异常 Ｈｂ 变异的一级结构基础．

To analyze the primary structure of a slow electrophoretic hemoglobin at Zhaoyuan city,Shandong,the purified abnormal chain was hydrolyzed by TPCK Trypsin,the abnormal peptide was separated by HPLC,and its amino acids composition and sequence were analyzed.Data showed the abnormal peptide was the same as normal β 41→59 peptide.No reaction took place between the abnormal peptide and CNBr.With the mass spectrophy analysis,the abnormal peptide showed a peak of mass charge ratio of 1 038 and the normal only a peak of mass charge ratio of 1 030.It appeard that the β 55 Met of the abnormal peptide was converted to the sulfoxide form β 55 Met·O.The change of primary structure was the structural basis of the slow electrophoretic Hb.It might be called Hb Zhaoyuan.