In vitro folding of inclusion body proteins
1996; Wiley; Volume: 10; Issue: 1 Linguagem: Inglês
10.1096/fasebj.10.1.8566547
ISSN1530-6860
Autores Tópico(s)Enzyme Production and Characterization
ResumoInsoluble, inactive inclusion bodies are frequently formed upon recombinant protein production in transformed microorganisms. These inclusion bodies, which contain the recombinant protein in an highly enriched form, can be isolated by solid/liquid separation. After solubilization, native proteins can be generated from the inactive material by using in vitro folding techniques. New folding procedures have been developed for efficient in vitro reconstitution of complex hydrophobic, multidomain, oligomeric, or highly disulfíde-bonded proteins. These protocols take into account process parameters such as protein concentration, catalysis of disulfide bond formation, temperature, pH, and ionic strength, as well as specific solvent ingredients that reduce unproductive side reactions. Modification of the protein sequence has been exploited to improve in vitro folding.—Rudolph, R., Lilie, H. In vitro folding of inclusion body proteins. FASEB J. 10, 49-56.
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