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PMID: 6212585 Published · ppublish English Journal Article

Purification and properties of a transcriptional activator. The cII protein of phage lambda.

The Journal of biological chemistry ·Vol. 257 ·No. 15 ·1982-08-10 ·Pages 9128-34

Ho Y, Lewis M, Rosenberg M

Abstract

We have purified the phage lambda transcriptional activator protein cII. The procedure described allows cII to be obtained in both high purity and yield, and thus allows detailed physical and chemical analysis. We demonstrate that cII in solution is a tetrameric protein and that it undergoes specific processing at its NH2-terminal end. In addition, the protein is characterized as to its molar extinction coefficient, molecular weight, amino acid composition, isoelectric point, alpha-helical content, and antigenic capability.

MeSH Terms
Amino Acids/analysis Bacteriophage lambda/analysis Electrophoresis, Polyacrylamide Gel Immunodiffusion Macromolecular Substances Molecular Weight Transcription Factors/isolation & purification Viral Proteins/isolation & purification
Chemicals
Amino Acids Macromolecular Substances Transcription Factors Viral Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ho Y
Lewis M
Rosenberg M
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1982-08-10
Pages
9128-34
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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