Lees S, Heeley J D, Cleary P F
Calcif Tissue Int. 1981;33(1):83-6. doi: 10.1007/BF02409417.
Dimensional stability of a demineralized bovine cortical bone sample was found in all media whether EDTA, saline or ethanol and water solutions or even 100% ethanol. A 6% volume shrinkage was observed, in strong contrast to the reported swelling for tail tendon fiber collagen. Sonic velocity was strongly dependent on the state and the medium, varying by a factor greater than 2. The medium appears to contribute strongly to the observed velocity suggesting that the Reuss formalism is applicable with the solid collagen skeleton as one component and the liquid in the pores as the second. Sonic anisotropy was noted although the intensity varied. The radial to axial velocity was greatest (0.93) in saline and least in 100% ethanol (0.80) indicating that the rigidity of the tissue influenced the character of sonic propagation. Two sets of intermolecular linkages are inferred. One set, in common with tendon collagen, controls the elastic properties. A second set in bone collagen maintains dimensional stability.
脱矿质牛皮质骨样本在所有介质中均表现出尺寸稳定性，无论是乙二胺四乙酸（EDTA）、生理盐水、乙醇与水溶液，甚至是100%乙醇。观察到有6%的体积收缩，这与报道的尾腱纤维胶原蛋白的肿胀情况形成强烈对比。声速强烈依赖于状态和介质，变化因子大于2。介质似乎对观察到的速度有很大贡献，这表明鲁氏（Reuss）形式适用于以固体胶原骨架为一个组分、孔隙中的液体为第二个组分的情况。尽管强度有所变化，但仍观察到声各向异性。在盐水中，径向与轴向速度之比最大（0.93），在100%乙醇中最小（0.80），这表明组织的刚性影响了声传播的特性。推断出两组分子间连接。一组与肌腱胶原蛋白相同，控制弹性特性。骨胶原蛋白中的第二组连接维持尺寸稳定性。
