SYNTHESIS AND CONFORMATIONAL PROPERTIES OF A RECOMBINANT C-PROPEPTIDEOF HUMAN TYPE-III PROCOLLAGEN

A cDNA was prepared that coded for the signal peptide of type III proc ollagen linked to the complete C-propeptide of the protein. The cDNA w as then used to express the protein in a baculovirus recombinant syste m. Recombinant protein was recovered as a trimer from the medium of tr ansfected cells in a yield of 1 to 2.5 mg per liter. Mapping of peptid e fragments with and without reduction indicated that the protein cont ained the expected interchain disulfide bonds. Analysis by circular di chroism suggested that the conformation of the protein corresponded to the native conformation. Therefore, the protein should be appropriate for further tests of its biological function and analysis of structur e by X-ray diffraction.