Muller S, Soussanieh A, Bouley J P, Reinbolt J, Van Regenmortel M H
Biochim Biophys Acta. 1983 Sep 14;747(1-2):100-6. doi: 10.1016/0167-4838(83)90127-9.
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.
通过固相肽合成制备了与组蛋白H4的羧基末端区域80 - 102相对应的四种重叠合成肽。通过在补体结合和酶联免疫吸附测定中抑制H4 - 抗H4反应来分析它们的抗原活性。一个抗原决定簇定位于H4分子的88 - 96位残基。在肽80 - 89和97 - 102中未发现抗原活性。发现由肽85 - 102诱导的抗体可与溶液中的游离H4结合，但不与染色质亚基结合，这表明核小体中H4的C末端区域缺乏可及性。发现第二个表位位于组蛋白H4的N末端区域1 - 53。
