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pubmed-article:1950768pubmed:abstractTextA protein with molecular weight of 60,000 that binds to the recombination signal sequence (RS) of the immunoglobulin J kappa segment was purified from the nuclear extract of a murine pre B cell line 38B9. This binding protein was found in lymphoid cell lines but not in non-lymphoid cell lines. The Kd value of the J kappa RS binding protein to the J kappa RS was 1 nM. The cDNA clone (RBP-2) was isolated based on partial amino-acid sequence of this protein. This cDNA encodes 526 amino-acid residues, and its sequence does not show extensive overall homology with any known proteins, but displays an interesting homology to a 40-residue region that is conserved among a subset of site specific recombinase (integrase family).lld:pubmed
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pubmed-article:1950768pubmed:pagination177-86lld:pubmed
pubmed-article:1950768pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1950768pubmed:articleTitleCloning and characterization of a protein binding to the J kappa recombination signal sequence of immunoglobulin genes.lld:pubmed
pubmed-article:1950768pubmed:affiliationDepartment of Medical Chemistry, Kyoto University Faculty of Medicine, Japan.lld:pubmed
pubmed-article:1950768pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1950768pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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