文章基本信息

标题：Isolation of antibodies specific to sickle hemoglobin by affinity chromatography using a synthetic peptide
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作者：N S Young ; J G Curd ; A Eastlake 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1975
卷号：72
期号：12
页码：4759-4763
DOI：10.1073/pnas.72.12.4759
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Antibodies to hemoglobin have been studied with a radioimmunoassay which employs [14C]carbamylated (= carbamolyated) hemoglobin S. An antiserum raised against hemoglobin S, which initially discriminated poorly between hemoglobins S and A, was fractionated by absorption to a column of Sepharose to which a synthetic peptide corresponding to the first 13 amino-acid residues of the beta chain of sickle hemoglobin had been covalently bound. A subpopulation of the antiserum was eluted from this column with 4 M guanidine - HC1. These antibodies showed binding to hemoglobin S but not to hemoglobin A and this interaction could be inhibited by the synthetic peptide. These antibodies, of demonstrated fine structural specificity, may be useful in the detection of sickle hemoglobin and in the study of its structure in solution.