Abstract
Five peptides from the NH2-terminal region of the beta chain of hemoglobin S, betaS (1-13), betaS (3-13), betaS (1-8), betaS (4-10), And betaS (4-8), have been synthesized by a rapid solid phase method based on the Merrifield procedure. In addition, one peptide, betaS (3-13), has also been synthesized by the original Merrifield method. We have shown that the products of the two methods are comparable, that gel filtration is a useful method for removing truncated fragments of the desired oligopeptide, and that measurement of the efficiency of coupling at each step is an important adjunct to amino acid analysis in determining purity. Peptides of the purity achieved by these methods may be used to fractionate antibodies to the native hemoglobin S, in the characterization of antigen-binding properties of specific antibodies, and in other studies of peptide-protein interactions.
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