Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 28 February 1964:
Vol. 143. no. 3609, pp. 960 - 961
DOI: 10.1126/science.143.3609.960
Prev | Table of Contents | Next

Articles

Ihermal Denaturation of Collagen in the Dispersed and Solid State

Jerome Gross 1

1 Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston

Thermal denaturation temperature of newly reconstituted collagen fibrils from rat tail tendons is 52°C compared with 42°C for neutral solutions. This suggests that the increase in concentration of collagen within the fibril increases the stability of the individual molecules. The absence of firm intermolecular bonds in these fibrils rules out crosslinking as an explanation for increased stability. "Aging" at 37°C up to 1 year raises the shrinkage temperature of reconstituted fibrous gels by 4° to 6°C and greatly increases resistance to dissolution at high temperature. The newly formed fibrils dissolve without shrinking, whereas older gels exhibit shrinkage before dissolution. Since nearly all extractable collagen is in the form of fibrillar aggregates in tissue, it is unlikely that thermal denaturation occurs at body temperature; therefore it could not be involved as a necessary stage in collagen resorption.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Ultrastructure of Collagen Thermally Denatured by Microsecond Domain Pulsed Carbon Dioxide Laser.
K. M. Kirsch, B. D. Zelickson, C. B. Zachary, and W. D. Tope (1998)
Arch Dermatol 134, 1255-1259
   Abstract »    Full Text »    PDF »
The role of warmup in muscular injury prevention.
M. R. Safran, W. E. Garrett JR, A. V. Seaber, R. R. Glisson, and B. M. Ribbeck (1988)
Am. J. Sports Med. 16, 123-129
   Abstract »    PDF »
Cross-Linking of Collagen.
M. L. Tanzer (1973)
Science 180, 561-566
   Abstract »    PDF »
Collagenolytic Activity of Intact and Necrotic Connective Tissue.
E. R. Goldstein, Y. M. Patel, and J. C. Houck (1964)
Science 146, 942-944
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)