BIOMECHANICAL AND ULTRASTRUCTURAL STUDIES ON ELASTIC WING TENDON FROM DOMESTIC-FOWL

  • 1 January 1977
    • journal article
    • research article
    • Vol. 123  (APR) , 369-387
Abstract
The interaction between collagen and elastin networks under conditions of load-extension was studied in the elastic wing tendon of the domestic fowl. The load-extension curves obtained were divided into 2 regions: the 1st region representing the ability of the tendon to undergo great extension at low tension and the 2nd representing a limit region where the collagen of the tendon appears to become fully extended. Following removal of the elastin network with pure elastase, only the 2nd region of the curve persisted, indicating that elastin is largely responsible for the mechanical events represented by the 1st region of the curve. The collagen network of tendons apparently is normally held in a folded conformational state by elastin, for elastase treatment results in elongation of tendons even in the absence of loading. Complete removal of elastin, and alignment of collagen bundles, were confirmed ultrastructurally in the elongated tendons. The breaking load of the elastase-treated tendons was also significantly reduced, indicating that an elastase-sensitive component is a limiting factor in determining the ultimate strength of the tendon.