| Literature DB >> 3036486 |
A W Thorne, P Sautiere, G Briand, C Crane-Robinson.
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.Entities:
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Year: 1987 PMID: 3036486 PMCID: PMC553496 DOI: 10.1002/j.1460-2075.1987.tb04852.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598