Muller S, Himmelspach K, Van Regenmortel M H
EMBO J. 1982;1(4):421-5. doi: 10.1002/j.1460-2075.1982.tb01185.x.
The C-terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130-135) corresponding to the sequence Ile-Arg-Gly-Glu-Arg-Ala ( IRGERA ) was prepared by solid-phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits. The antigenic activity of the synthetic peptide IRGERA was found to be very similar to that of the natural CN3 fragment (residues 121-135), and it inhibited the H3-anti H3 reaction in complement fixation, solid-phase radioimmunoassay, and enzyme-linked immunosorbent assay. Antibodies induced by IRGERA were found to bind equally well to IRGERA coupled to hemocyanin, to the intact H3 molecule, and to chromatin subunits (nucleosomes and core particles). The results demonstrate that the C-terminal hexapeptide of histone H3 is located at the surface of chromatin subunits and agree with current models proposed for the spatial organization of the chromatin core particle.
鸡红细胞组蛋白H3的C末端六肽（第130 - 135位氨基酸残基），其对应序列为异亮氨酸-精氨酸-甘氨酸-谷氨酸-精氨酸-丙氨酸（IRGERA），通过固相肽合成法制备，与牛血清白蛋白偶联后，用于在兔体内诱导抗体。发现合成肽IRGERA的抗原活性与天然CN3片段（第121 - 135位氨基酸残基）非常相似，并且在补体结合、固相放射免疫测定和酶联免疫吸附测定中抑制H3抗H3反应。发现由IRGERA诱导的抗体与偶联血蓝蛋白的IRGERA、完整的H3分子以及染色质亚基（核小体和核心颗粒）结合的效果相同。结果表明组蛋白H3的C末端六肽位于染色质亚基表面，与目前提出的染色质核心颗粒空间组织模型相符。
