Process for the biocatalytic, correct chain folding of denatured recombinant fusion proteins

摘要

Denatured recombinant fusion proteins are correctly folded in the presence of a heat shock protein which acts according to the functional principle of the bacterial GroEL or of the equivalent mitochondrial component Hsp60, and of ATP. After cleaving off the foreign sequence, biologically and medically interesting proteins are obtained in the correct conformation.