Abstract
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.
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Fine, M., Daniel, V., Levanon, A. et al. 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. Biotechnol Tech 7, 769–774 (1993). https://doi.org/10.1007/BF00153742
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DOI: https://doi.org/10.1007/BF00153742