A short-time refolding procedure that dramatically increases the yields of recombinant monomeric carp growth hormone and its Cys123Ala mutant: Implications for other proteins with an unpaired number of cysteine residues

Autor:	Arieh Gertler, Violet Daniel, Mira Fine, A. Levanon
Rok vydání:	1993
Předmět:	biology Mutant Biological activity biology.organism_classification Applied Microbiology and Biotechnology Biochemistry law.invention chemistry.chemical_compound chemistry law Urea Extracellular Recombinant DNA Carp Receptor Cysteine
Zdroj:	Biotechnology Techniques. 7:769-774
ISSN:	1573-6784 0951-208X
DOI:	10.1007/bf00153742
Popis:	Recombinant carp growth hormone and its Cys123Ala analogue were refolded in 4.5 M urea, pH 11.3 in the presence of 0.1 mM cysteine. Shortening of the refolding process from 48 h to 1 h resulted in a 30 to 40 fold increase in yield of the biologically active monomers, and lowered dimerization and oligomerization. A similar short-time refolding procedure was also found to be advantageous with other structurally different, non-related proteins, such as the extracellular domains of rabbit and bovine prolactin receptors.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9b3680e2ba622702a4cdd0193bbe026d https://doi.org/10.1007/bf00153742 Zobrazit plný text záznamu Full text from SpringerLink