Anderson J C, Labedz R I, Kewley M A
Biochem J. 1977 Nov 1;167(2):345-51. doi: 10.1042/bj1670345.
The formation of collagen fibrils under physiological conditions of ionic strength, pH and temperature was markedly affected by the presence of small amounts of bovine tendon glycoprotein. The absorbance of the gels at 400 nm was decreased, and they took longer to form. Over the range of concentration tested, the negative specific absorbance, -delta Asp., and the specific retardation, Rsp., both increased with the glycoprotein to collagen ratio. When added during the nucleation phase, glycoprotein was still able to exert its effect almost fully, and so must act to inhibit the later stages of fibril formation. Several pieces of evidence showed that glycoprotein acts via a weak binding to the collagen molecule. Electron microscopy established that fibrils formed in the presence of glycoprotein had a normal cross-striation pattern, but were significantly thinner than fibrils formed in control gets. The results suggest that glycoprotein could act in tissues to help regulate the diameter of collagen fibrils.
在离子强度、pH值和温度的生理条件下，少量牛腱糖蛋白的存在显著影响胶原纤维的形成。凝胶在400nm处的吸光度降低，并且形成所需时间更长。在所测试的浓度范围内，负比吸光度（-ΔAsp.）和比延迟（Rsp.）均随糖蛋白与胶原蛋白的比例增加而增加。当在成核阶段添加时，糖蛋白仍然能够几乎完全发挥其作用，因此其作用必定是抑制纤维形成的后期阶段。几条证据表明，糖蛋白通过与胶原分子的弱结合发挥作用。电子显微镜显示，在糖蛋白存在下形成的纤维具有正常的横纹模式，但明显比在对照凝胶中形成的纤维细。结果表明，糖蛋白可以在组织中发挥作用，以帮助调节胶原纤维的直径。
