Thorne A W, Sautiere P, Briand G, Crane-Robinson C
EMBO J. 1987 Apr;6(4):1005-10. doi: 10.1002/j.1460-2075.1987.tb04852.x.
Ubiquitinated histone H2B (uH2B) has been purified from both calf and pig thymus by exclusion chromatography in 7 M urea. Digestion of uH2B with Staphylococcus aureus V8 protease yielded the peptide 114-125 containing the ubiquitin moiety. Further digestion of this peptide with trypsin removed the ubiquitin and three H2B residues from the N-terminus. Edman degradations of both peptides established that ubiquitin is attached to the epsilon-amino group of lysine 120 in both calf and pig uH2B by an iso-peptide bond to the C-terminal glycine 76 of ubiquitin.
泛素化组蛋白H2B（uH2B）已通过在7M尿素中进行排阻色谱法从小牛胸腺和猪胸腺中纯化出来。用金黄色葡萄球菌V8蛋白酶消化uH2B得到了包含泛素部分的114 - 125肽段。用胰蛋白酶进一步消化该肽段，从N端去除了泛素和三个H2B残基。对这两个肽段进行的埃德曼降解确定，在小牛和猪的uH2B中，泛素均通过与泛素C端甘氨酸76形成异肽键，连接到赖氨酸120的ε-氨基上。
