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Thermal Stability of Type I and Type III Procollagens from Normal Human Fibroblasts and from a Patient with Osteogenesis Imperfecta
Leena Peltonen, Aarno Palotie, Toshihiko Hayashi and Darwin J. Prockop
Proceedings of the National Academy of Sciences of the United States of America
Vol. 77, No. 1, [Part 2: Biological Sciences] (Jan., 1980), pp. 162-166
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/8162
Page Count: 5
You can always find the topics here!Topics: Fibroblasts, Collagens, Thermal stability, Gels, Biochemistry, Centrifugation, Electrophoresis, Osteogenesis imperfecta, Amino acids, Dichroism
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1980 National Academy of Sciences