Separation of copurifying GroEL from glutathione-S-transferase fusion proteins

Protein Expression and Purification

Volumn 20, Issue 1, 2000, Pages 45-47

  Rohman, Mattias ^a   Harrison Lavoie, Kimberly J ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN EXPRESSION;

BACTERIA (MICROORGANISMS);

EID: 0033815536     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1271     Document Type: Article

References (7)

1. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
2. A method for the separation of GST fusion proteins from co-purifying GroEL
3. Identification of in vivo substrates of the chaperonin GroEL
4. Residues in the chaperonin GroEL required for polypeptide binding and release
5. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
6. Purified chaperonin 60 (GroEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
7. Cleavage of structural proteins during the assembly of the head bacteriophage T4