Abstract
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.
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Forster, S.J., Freedman, R.B. Catalysis by protein disulphide-isomerase of the assembly of trimeric procollagen from procollagen polypeptide chains. Biosci Rep 4, 223–229 (1984). https://doi.org/10.1007/BF01119657
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DOI: https://doi.org/10.1007/BF01119657