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

Journal Article · Mon Dec 01 04:00:00 EST 1975 · Proc. Natl. Acad. Sci. U.S.A., v. 72, no. 12, pp. 4759-4763

DOI:https://doi.org/10.1073/pnas.72.12.4759· OSTI ID:4061021

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

Antibodies to hemoglobin have been studied with a radioimmunoassay which employs [$sup 14$C]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 $beta$ 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. (auth)

• Research Organization: National Inst. of Health, Bethesda, MD
• Sponsoring Organization: USDOE
• NSA Number: NSA-33-029855
• OSTI ID: 4061021
• Journal Information: Proc. Natl. Acad. Sci. U.S.A., v. 72, no. 12, pp. 4759-4763, Journal Name: Proc. Natl. Acad. Sci. U.S.A., v. 72, no. 12, pp. 4759-4763; ISSN PNASA
• Country of Publication: United States
• Language: English

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