Abstract
Four overlapping synthetic peptides corresponding to the carboxy-terminal region 80–102 of histone H4 were prepared by solid-phase peptide synthesis. Their antigenic activity was analysed by inhibition of the H4-anti-H4 reaction in complement fixation and enzyme-linked immunosorbent assay. One antigenic determinant was localized in residues 88–96 of the H4 molecule. No antigenic activity was found in peptides 80–89 and 97–102. Antibodies induced by peptide 85–102 were found to bind to free H4 in solution but not to chromatin subunits, suggesting a lack of accessibility of the C-terminal region of H4 in nucleosomes. A second epitope was found to be situated in the N-terminal region 1–53 of histone H4.
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More From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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