Chambers C A, Shuttleworth C A, Ayad S, Grant M E
Biochem J. 1984 Jun 1;220(2):385-94. doi: 10.1042/bj2200385.
The collagenous components were investigated in peptic digests of developing bovine nuchal ligament. Types I and III collagen were the major species isolated, but the presence of types IV, V and VI was also shown. Changes in the pepsin-susceptibility of nuchal ligament during foetal development were observed. CNBr-cleavage peptide analysis indicated that type I collagen became cross-linked rapidly, as evidenced by the lack of alpha 1(I)CB6. At present it is not clear if this decrease in pepsin-susceptibility is due to cross-linking of collagen, to increased deposition of elastin, or to both. Quantification of collagen types I and III was shown to depend on the method used. When pepsin-solubilized material was examined an apparent increase in type III collagen with respect to foetal age was observed, whereas when CNBr digests of intact ligament were examined a relatively constant amount of type III collagen (approx. 24%) was found. The constant amount of type III collagen observed during foetal development changed at birth and increased in mature nuchal ligament to represent approx. 45% of the total collagen.
对发育中的牛项韧带的胃蛋白酶消化物中的胶原成分进行了研究。分离出的主要胶原类型为I型和III型，但也发现了IV型、V型和VI型胶原的存在。观察到胎儿发育过程中项韧带对胃蛋白酶敏感性的变化。溴化氰裂解肽分析表明，I型胶原迅速发生交联，这可通过缺乏α1(I)CB6得以证明。目前尚不清楚这种胃蛋白酶敏感性的降低是由于胶原交联、弹性蛋白沉积增加，还是两者兼而有之。I型和III型胶原的定量结果显示取决于所使用的方法。当检查胃蛋白酶溶解的物质时，观察到III型胶原相对于胎儿年龄明显增加，而当检查完整韧带的溴化氰消化物时，发现III型胶原的含量相对恒定（约24%）。在胎儿发育过程中观察到的III型胶原的恒定含量在出生时发生变化，并在成熟的项韧带中增加，约占总胶原的45%。
