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

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

Research output: Contribution to journalArticlepeer-review

84 Scopus citations

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 - 1988
Externally publishedYes

ASJC Scopus subject areas

  • General

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