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pubmed-article:2511556pubmed:abstractTextA protein that binds to the recombination signal sequence (RS) of the immunoglobulin J kappa segment was purified almost to homogeneity from the nuclear extract of a murine pre-B cell line 38B9. A similar binding protein was found in lymphoid cell lines but not in non-lymphoid cell lines. The binding activity was associated with a polypeptide with a molecular weight of 60,000. DNase I footprinting analysis demonstrated that this binding protein interacted with the heptamer and several 3' bases close to the heptamer. The Kd value of the J kappa RS binding protein to the J kappa RS was 1 nM. One base substitution in the heptamer of the J kappa RS greatly reduced the affinity of the J kappa RS binding protein. The high specificity of the binding site of the J kappa RS binding protein suggests that this protein may be involved in V-J recombination.lld:pubmed
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pubmed-article:2511556pubmed:articleTitlePurification and characterization of a protein that binds to the recombination signal sequence of the immunoglobulin J kappa segment.lld:pubmed
pubmed-article:2511556pubmed:affiliationDepartment of Medical Chemistry, Kyoto University Faculty of Medicine, Japan.lld:pubmed
pubmed-article:2511556pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2511556pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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