Isolation of antibodies specific to sickle hemoglobin by affinity chromatography using a synthetic peptide

N. S. Young, J. G. Curd, A. Eastlake, B. Furie, A. N. Schechter

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Abstract

Antibodies to hemoglobin have been studied with a radioimmunoassay which employs [ 14C] carbamylated (= carbamoylated) 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 β chain of sickle hemoglobin had been covalently bound. A subpopulation of the antiserum was eluted from this column with 4 M guanidine. HCL. 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.

Original languageEnglish
Pages (from-to)4759-4763
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume72
Issue number12
DOIs
StatePublished - 1975

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