[Structure and properties of the collagen complex of tendons following disorganization of the connective tissue ground substance].
Scanning and transmission electron microscopy, as well as physicochemical research methods were used to study the structure and characteristics of the tendon collagen complex during enzymatic distintegration of basal substance of connective tissue. Disintegration of basal substance was shown to be accompanied by substantial derangement of the microstructure of collagen fibers and to entail changes in the modulus of elasticity and residual deformation of the collagen complex with its ability to hydration in a aqueous medium to be increased. The physiochemical and rheological characteristics of the collagen complex were found to be affected to a considerable degree by structural changes occurring in collagen fibers. These changes consist in the formation of a retiform structure containing numerous macrospores.
D000125:Achilles Tendon / Q000032:analysis / Q000648:ultrastructure*; D000328:Adult; D001696:Biomechanical Phenomena; D003094:Collagen; D004548:Elasticity; D006595:Hexosamines / Q000032:analysis; D006801:Humans; D008855:Microscopy, Electron, Scanning; D008875:Middle Aged; D013696:Temperature; D014867:Water / Q000032:analysis
D006595:Hexosamines; D014867:Water; D003094:Collagen
Struktura i svoĭstva kollagenovogo kompleksa sukhozhiliia pri dezorganizatsii osnovnogo veshchestva soedinitel'noĭ tkani.