Collagen crosslinks and their relationship to the thermal properties of calf tendons
| Autor: | Lyndon B. Kurth, Ronald Kuypers, N.L. King, Douglas J. Horgan |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Collagen crosslink
Hot Temperature Thermal transition Biophysics macromolecular substances Isometric exercise Biochemistry Calf muscles Tendons chemistry.chemical_compound medicine Animals Pyrroles Amino Acids neoplasms Molecular Biology Pyridinoline Calorimetry Differential Scanning Chemistry technology industry and agriculture musculoskeletal system Tendon Cross-Linking Reagents medicine.anatomical_structure Cattle Collagen |
| Zdroj: | Archives of Biochemistry and Biophysics. 281:21-26 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(90)90407-p |
| Popis: | The hydrothermal isometric tension and thermal transition temperature of collagen were determined in tendons from three different calf muscles. The levels of the nonreducible collagen crosslink, pyridinoline, and the collagen-associated Ehrlich chromogen were also measured in the three tendons. The reducible collagen crosslinks, hydroxylysinonorleucine, dihydroxylysinonorleucine, and histidinohydroxymerodesmosine were measured in two tendons. The thermal properties and levels of crosslinks were found to vary considerably between the different tendons, and also at different sites in two of the tendons. A strong correlation was observed between the thermal transition temperatures and the hydrothermal isometric tensions of the nine tendon sites examined. Both thermal properties correlated with the concentration of both pyridinoline and Ehrlich chromogen. The analogous behavior of the collagen-associated Ehrlich chromogen and the pyridinoline crosslink supports the role of the Ehrlich chromogen as a nonreducible crosslink. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|