Catalysis by protein disulphide-isomerase of the assembly of trimeric procollagen from procollagen polypeptide chains.
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.
D000818:Animals; D002250:Carbon Radioisotopes; D002642:Chick Embryo; D004229:Dithiothreitol / Q000494:pharmacology; D005978:Glutathione / Q000494:pharmacology; D007535:Isomerases / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D011347:Procollagen / Q000302:isolation & purification / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D013710:Tendons / Q000378:metabolism
D002250:Carbon Radioisotopes; D046911:Macromolecular Substances; D011347:Procollagen; D012967:Sodium Dodecyl Sulfate; D007535:Isomerases; D019704:Protein Disulfide-Isomerases; D005978:Glutathione; D004229:Dithiothreitol