| Literature DB >> 2481233 |
T R Hebbes1, C H Turner, A W Thorne, C Crane-Robinson.
Abstract
Antibodies that recognise proteins bind to epitopes of varying size, but a grouping of the order of six amino acids, contiguous or not, is regarded as a typical number. By using as immunogen a highly abundant and universal eukaryotic nuclear protein (histone H4) modified in a manner not typical of secreted proteins (acetylation of lysine side chains), antiserum has been raised in rabbits having the single amino acid epsilon-N-acetyl lysine as the recognition epitope. The affinity-purified antibody should be useful for studying the functional role of this modification. The methodology has potential for raising antibodies to other types of post-translationally modified proteins.Entities:
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Year: 1989 PMID: 2481233 DOI: 10.1016/0161-5890(89)90143-0
Source DB: PubMed Journal: Mol Immunol ISSN: 0161-5890 Impact factor: 4.407