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

Recombinant carp growth hormone and its Cys123Ala analogue were refold ed in 4.5 M urea, pH 11.3 in the presence of 0.1 mM cysteine. Shorteni ng of the refolding process from 48 h to 1 h resulted in a 30 to 40 fo ld increase in yield of the biologically active monomers, and lowered dimerization and oligomerization. A similar short-time refolding proce dure was also found to be advantageous with other structurally differe nt, non-related proteins, such as the extracellular domains of rabbit and bovine prolactin receptors.