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NF-kappa B protein purification from bovine spleen: nucleotide stimulation and binding site specificity.

1988; National Academy of Sciences; Volume: 85; Issue: 23 Linguagem: Inglês

10.1073/pnas.85.23.8825

1091-6490

Michael J. Lenardo, Anna A. Kuang, Ann Gifford, David Baltimore,

Immune Response and Inflammation

The activity of the enhancer for the kappa immunoglobulin light chain gene critically depends on the presence in the nucleus of the NF-kappa B protein. We purified NF-kappa B 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-kappa B as well as that from human and murine B- or T-lymphoid cell extracts was dramatically stimulated by nucleoside triphosphates. This effect distinguished NF-kappa B from a related factor, H2-TF1. Purified NF-kappa B interacted efficiently with regulatory sequences that function during either B- or T-lymphocyte activation, including the human immunodeficiency virus enhancer and a NF-kappa B binding site we detected in the interleukin 2 enhancer.