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JBC, Vol. 251, Issue 5, 1290-1295, Mar, 1976

Antibodies to an NH2-terminal fragment of betaS globin. II. Specificity and isolation of antibodies for the sickle mutation

J. G. Curd, N. S. Young and A. N. Schechter

The immunochemical specificity of an antiserum produced to an NH2-terminal 55-residue polypeptide fragment of the betaS globin, betaS(1-55), was analyzed with a radioimmunoassay using the radioiodinated fragment as a tracer. These studies show that most of the antibodies have comparable reactivity with betaS(1-55), betaA(1-55), betaS globin, betaA globin, HbS, and HbA. However, the antiserum contains some antibodies which react only with the species derived from HbS. These "S" -specific antibodies were isolated by absorption of the serum on a column of betaA(1-55) coupled covalently to Sepharose. The S-specific antibodies have markedly diminished reaction with betaA(1-55) and HbA. The S specificity was localized to the valine substitution at position 6 of the beta globin, as shown by inhibition of the binding of the radiolabeled fragment to S-specific antibodies by the synthetic peptide betaS(1-13). These antibodies, which appear monospecific, can be used to study the conformation of the NH2-terminal region of the beta chain of HbS.
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