招远市异常血红蛋白的分子结构  

MOLECULAR STRUCTURE OF AN ABNORMAL HEMOGLOBIN IN ZHAO YUAN

作　　者：陈培勋[1] 王广华 夏其昌[2] 徐来根[2] 鲁道远[3] 张春源[3] 刘在贵[4] 王桂兰[4] 

机构地区：[1]青岛医学院生物化学教研室,青岛266021 [2]中国科学院生物化学研究所 [3]青岛医学院附属医院血液病研究 [4]滨州医学院生物化学教研室

出　　处：《青岛医学院学报》1996年第4期302-305,共4页Acta Academiae Medicinae Qingdao Universitatis

基　　金：山东省卫生厅科研基金资助课题

摘　　要：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。Objective To study the molecular structure of an abnormal hemoglobin discovered in Zhao Yuan. Method The purified abnormal p chains were hydrolyzed by trypsin and analyzed with HPLC- Result The normal peptide I was replaced by a peptide I in the abnormal (3 chain. Both peptide I and I were 19 peptides having the same amino acid sequence with 41~59 segment in normal (3 chain. The P 55 Met in peptide 1 could not react with CNBr when both peptide I and I were treated with CNBr. During mass spectrography analysis, the peptide I showed a mass charge ratio peak of 1030, the peptide I showed a mass charge ratio peak of 1038. Conclusion The abnormal hemoglobin discovered in Zhao Yuan is due to the transformation of p 55 Met into hydroxylated methionine.

关 键 词：血红蛋白异常 氨基酸序列 光谱分析 分子结构 

分 类 号：R556.7[医药卫生—血液循环系统疾病] Q513.4[医药卫生—内科学]