Wouters D, Sautiere P, Biserte G
Eur J Biochem. 1978 Oct;90(2):231-9. doi: 10.1111/j.1432-1033.1978.tb12595.x.
The complete amino acid sequence (125 residues) of sea urchin histone H2A has been established by structural studies of peptides derived from tryptic and chymotryptic cleavage of the maleylated protein and from thermolysin cleavage of the intact protein. By comparison with calf homologous histone, the basic amino-terminal and carboxy-terminal parts of the protein show 11 substitutions and 4 deletions. The remainder of the sequence, mostly hydrophobic, is almost completely unchanged.
通过对马来酰化蛋白经胰蛋白酶和糜蛋白酶裂解产生的肽段以及完整蛋白经嗜热菌蛋白酶裂解产生的肽段进行结构研究，已确定了海胆组蛋白H2A的完整氨基酸序列（125个残基）。与小牛同源组蛋白相比，该蛋白的碱性氨基末端和羧基末端部分有11个取代和4个缺失。序列的其余部分大多是疏水的，几乎完全未变。
