Type-I procollagen, 14C-biosynthetically labelled, was reduced under denaturing and non-denaturing conditions. Reoxidation to disulphide-linked trimers occurred with non-denatured chains in the presence of an oxidant system containing oxidized and reduced glutathione. Dimeric intermediates were not detected. This reoxidation was accelerated by homogeneous beef liver protein disulphide-isomerase.
Catalysis by protein disulphide-isomerase of the assembly of trimeric procollagen from procollagen polypeptide chains
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Simon J. Forster, Robert B. Freedman; Catalysis by protein disulphide-isomerase of the assembly of trimeric procollagen from procollagen polypeptide chains. Biosci Rep 1 March 1984; 4 (3): 223–229. doi: https://doi.org/10.1007/BF01119657
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