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①目的 了解发现于招远市异常血红蛋白的分子结构。②方法 纯化的异常β链经胰蛋白酶水解,用高效液相层析仪、质谱仪分析水解得到的肽。③结果 异常β链中肽Ⅱ取代正常β链的肽Ⅰ、肽Ⅰ、Ⅱ均为19肽,氨基酸序列与正常β链41—59相同。采用溴化氰分别处理肽Ⅰ或肽Ⅱ,肽Ⅱ的β55Met不反应。质谱分析结果表明,肽Ⅰ质荷比为1030峰,而肽Ⅱ,由质荷比为1038的峰替代肽I的1030峰。④结论招远市发现的异常血红蛋白有异常β链,其分子结构的异常是β55Met转变为羟基化蛋氨酸所致。
① Objective To understand the molecular structure of abnormal hemoglobin found in Zhaoyuan City. ② method of purification of abnormal β chain by trypsin hydrolysis, high performance liquid chromatography, mass spectrometry analysis of the resulting peptide. ③ Abnormal results β chain peptide Ⅱ instead of the normal β-chain peptide Ⅰ, peptide Ⅰ, Ⅱ are 19 peptides, the amino acid sequence and the normal β-chain 41-59 the same. Treatment of peptide I or peptide II with cyanogen bromide, respectively, does not respond to β55Met of peptide II. The results of mass spectrometry showed that the mass-to-charge ratio of peptide I was 1030, while that of peptide II, the 1030 peak of peptide I was replaced by the mass-to-charge ratio of 1038. ④ Conclusion Abnormal hemoglobin found in Zhaoyuan City has abnormal β chain. The abnormality of its molecular structure is caused by the change of β55Met to hydroxylated methionine.