Laine B, Kmiecik D, Sautiere P, Biserte G
Biochimie. 1978;60(2):147-50. doi: 10.1016/s0300-9084(78)80747-0.
The complete amino acid sequence (128 residues) of the chicken erythrocyte histone H2A was deduced from the data provided by structural studies on the tryptic peptides from the maleylated histone and of the peptides obtained by thermolysin digestion of the native protein. The sequence of chicken histone H2A differs from the calf homologous histone by the deletion of one residue of histidine at position 123 or 124 and three conservative substitutions: a residue of serine replaces a residue of threonine at position 16, a residue of aspartic acid replaces a residue of glutamic acid at position 121 and a residue of alanine replaces a residue of glycine at position 128.
鸡红细胞组蛋白H2A的完整氨基酸序列（128个残基）是根据对马来酰化组蛋白的胰蛋白酶肽段以及天然蛋白经嗜热菌蛋白酶消化得到的肽段的结构研究数据推导出来的。鸡组蛋白H2A的序列与小牛同源组蛋白的不同之处在于，在第123或124位缺失了一个组氨酸残基，以及三个保守性替换：在第16位，一个丝氨酸残基取代了一个苏氨酸残基；在第121位，一个天冬氨酸残基取代了一个谷氨酸残基；在第128位，一个丙氨酸残基取代了一个甘氨酸残基。
