Oakes V W, Bialkower B
J Anat. 1977 Apr;123(Pt 2):369-87.
The interaction between collagen and elastin networks under conditions of load-extension has been studied in the elastic wing tendon of the domestic fowl. The load-extention curves obtained could be divided into two regions, the first region representing the ability of the tendon to undergo great extension at low tension, the second 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 second region of the curve persisted, indicating that elastin is largely responsible for the mechanical event represented by the first 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 breading load of the elastase-treated tendons was also significangly reduced, indicating that an elastase-sensitive component is a limiting factor in determining the ultimate strength of the tendon.
在家禽的弹性翅腱中，研究了在拉伸载荷条件下胶原蛋白和弹性蛋白网络之间的相互作用。所获得的拉伸载荷曲线可分为两个区域，第一个区域表示腱在低张力下能够进行大幅度伸展的能力，第二个区域表示一个极限区域，此时腱中的胶原蛋白似乎已完全伸展。仅用纯弹性蛋白酶去除弹性蛋白网络后，曲线的第二个区域仍然存在，这表明弹性蛋白在很大程度上决定了曲线第一个区域所代表的力学过程。腱中的胶原蛋白网络显然通常由弹性蛋白保持在折叠的构象状态，因为即使在没有加载的情况下，弹性蛋白酶处理也会导致腱伸长。在伸长的腱中，通过超微结构证实了弹性蛋白的完全去除和胶原束的排列。弹性蛋白酶处理过的腱的断裂载荷也显著降低，这表明对弹性蛋白酶敏感的成分是决定腱极限强度的一个限制因素。
