Thermal stability of type I and type III procollagens from normal human fibroblasts and from a patient with osteogenesis imperfecta.
Type I and type III procollagens were isolated from the medium of human fibroblast cultures in amounts adequate for examination by circular dichroism. Type I procollagen had a spectrum similar to that of type I procollagen and collagen from chicken embryos. The human type III procollagen showed a red shift not seen in type III collagen from calf skin. The midpoint (tm) for the helix-to-coil transition for both human procollagens was 40 degrees C. the same tm values were obtained with type I and type III procollagens synthesized by fibroblasts from a patient with osteogenesis imperfecta. Type I procollagen synthesized by the patient's fibroblasts, however, tended to aggregate more readily than type I procollagen from normal human fibroblasts, apparently because of a structural alteration of the protein.
D002478:Cells, Cultured; D002942:Circular Dichroism; D006358:Hot Temperature; D006801:Humans; D010013:Osteogenesis Imperfecta / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011347:Procollagen / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation
D010446:Peptide Fragments; D011347:Procollagen