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

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

Research output: Contribution to journalArticle

83 Citations (Scopus)

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
StatePublished - 1988
Externally publishedYes

Fingerprint

Immunoglobulin Light Chain Genes
Lymphocyte Activation
Cell Extracts
Nucleosides
Sodium Dodecyl Sulfate
Interleukin-2
Spleen
Nucleotides
Binding Sites
HIV
Lymphocytes
T-Lymphocytes
DNA
Proteins
IgA receptor
triphosphoric acid
polyacrylamide gels

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

NF-κB protein purification from bovine spleen : Nucleotide stimulation and binding site specificity. / Lenardo, M. J.; Kuang, Anna; Gifford, A.; Baltimore, D.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 23, 1988, p. 8825-8829.

Research output: Contribution to journalArticle

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