Physical characterization of the purified CCAAT transcription factor, alpha-CP1.

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Article

Physical characterization of the purified CCAAT transcription factor, alpha-CP1.

The Journal of biological chemistry - 5 Aug 1990

Kim C G, Sheffery M

Abstract excerpt

We have used DNA sequence affinity chromatography previously to purify a murine erythroid cell nuclear factor termed alpha-CP1. This promoter selective transcription factor is a heterotypic CCAAT factor composed of at least seven polypeptides with Mr values that range from 27,000 to 38,000. Peptide mapping experiments reported here show that these seven polypeptides fall into three distinct classes (alpha, beta,...

Topics

Animals
Base Sequence
CCAAT-Enhancer-Binding Proteins
Cell Line
Cell Nucleus
Centrifugation, Density Gradient
Chromatography, Gel
DNA, Neoplasm
DNA-Binding Proteins
Deoxyribonuclease I
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Molecular Weight

Mutation

Oligonucleotide Probes

Peptide Mapping

Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 2376599

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2376599-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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