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Autoimmune antigen Ku is enriched on oligonucleotide columns distinct from those containing the octamer binding protein DNA consensus sequence
Author(s) -
Quinn J.P.,
Farina A.R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80979-d
Subject(s) - histone octamer , oligonucleotide , dna , sequence (biology) , consensus sequence , dna binding protein , dna sequencing , chemistry , microbiology and biotechnology , computational biology , biology , biochemistry , gene , base sequence , transcription factor , nucleosome , histone
During purification of the AP1 complex from the T cell line MLA144 we enriched for a complex which bound to an oligonucleotide column containing the AP1 DNA consensus sequence and co‐eluted with a fraction required for AP1 binding activity. This complex although co‐eluting with AP1 binding activity had previously been determined to be non‐specific in its DNA binding properties. Further investigation determined that the complex was a heterodimer of 85 and 70 kDa which was antigenically related to the autoimmune antigen Ku. It is important to be aware of the abundance and avidity of the Ku complex to bind oligonucleotide columns when purifying sequence specific binding proteins.