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. 1987 Apr;6(4):1005–1010. doi: 10.1002/j.1460-2075.1987.tb04852.x

The structure of ubiquitinated histone H2B.

A W Thorne, P Sautiere, G Briand, C Crane-Robinson
PMCID: PMC553496  PMID: 3036486

Abstract

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.

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Selected References

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