NF-κB protein purification from bovine spleen: Nucleotide stimulation and binding site specificity

M. J. Lenardo, A. Kuang, A. Gifford, D. Baltimore

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    Abstract

    The activity of the enhancer for the κ immunoglobulin light chain gene critically depends on the presence in the nucleus of the NF-κB protein. We purified NF-κB over 50,000-fold and identified two protein species, 42 and 44 kDa, that could be eluted and renatured from a sodium dodecyl sulfate/polyacrylamide gel to give specific DNA-binding activity. Binding of the purified bovine NF-κB as well as that from human and murine B- or T-lymphoid cell extracts was dramatically stimulated by nucleoside triphosphates. This effect distinguished NF-κB from a related factor, H2-TF1. Purified NF-κB interacted efficiently with regulatory sequences that function during either B- or T-lymphocyte activation, including the human immunodeficiency virus enhancer and a NF-κB binding site we detected in the interleukin 2 enhancer.

    Original languageEnglish (US)
    Pages (from-to)8825-8829
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume85
    Issue number23
    DOIs
    StatePublished - Jan 1 1988

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