[Structure and mechanical properties of dermatosparactic collagen (author's transl)].
Dermatosparactic calf-tail-tendon-collagen was investigated by mechanical measurements, electron microscopy and x-ray diffraction. We suppose, that the tensile strength decrease of the fibres is due to the irregular aggregation of subfibrils to fibrils. The x-ray diagram of the fibre is not influenced by state of disorder. Cyclic extension of dermatosparactic collagen leads to a higher increase in tensile strength than in the case of normal calf tendon. The effect might be due to the increase of fibril- and area-density resulting in an augmentation of crosslinks.
D000818:Animals; D002417:Cattle; D002418:Cattle Diseases; D003094:Collagen; D003095:Collagen Diseases / Q000662:veterinary*; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D011487:Protein Conformation; D012871:Skin Diseases / Q000662:veterinary; D013710:Tendons / Q000032:analysis*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D003094:Collagen
Struktur und mechanische Eigenschaften dermatosparaktischen Kollagens.