Thermal stability of type I and type III procollagens from normal human fibroblasts and from a patient with osteogenesis imperfecta. Academic Article

abstract

• 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.

authors

• Prockop, Darwin

published proceedings

• Proc Natl Acad Sci U S A

altmetric score

• 6

author list (cited authors)

• Peltonen, L., Palotie, A., Hayashi, T., & Prockop, D. J.

citation count

• 62

complete list of authors

• Peltonen, L||Palotie, A||Hayashi, T||Prockop, DJ

publication date

• January 1980

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Cells, Cultured
• Circular Dichroism
• Hot Temperature
• Humans
• Osteogenesis Imperfecta
• Peptide Fragments
• Procollagen
• Protein Conformation
• Protein Denaturation

PubMed Central ID

• 6928611

Digital Object Identifier (DOI)

• 10.1073/pnas.77.1.162

start page

• 162

end page

• 166

volume

• 77

issue

• 1

URL

• http://dx.doi.org/10.1073/pnas.77.1.162