Cronlund A L, Smith B D, Kagan H M
Connect Tissue Res. 1985;14(2):109-19. doi: 10.3109/03008208509015017.
The binding of highly purified bovine aortic lysyl oxidase to native fibrils of type I collagen has been measured by assay of unbound lysyl oxidase activity in the supernatants of enzyme-collagen mixtures after centrifugation. The apparent binding affinity of lysyl oxidase for native fibrils is quite similar to that for fibrils prepared from pepsin- or chymotrypsin-digested type I collagen, demonstrating that the enzyme binds to the triple-helical portion of collagen molecules. The data also indicate that the enzyme binds predominantly to the fibrillar surface. The results suggest that lysyl oxidase initiates crosslink formation at an early stage in collagen fibrillogenesis.
通过对酶 - 胶原蛋白混合物离心后的上清液中未结合的赖氨酰氧化酶活性进行测定，来测量高度纯化的牛主动脉赖氨酰氧化酶与I型胶原蛋白天然纤维的结合情况。赖氨酰氧化酶对天然纤维的表观结合亲和力与对由胃蛋白酶或胰凝乳蛋白酶消化的I型胶原蛋白制备的纤维的亲和力非常相似，这表明该酶与胶原蛋白分子的三螺旋部分结合。数据还表明，该酶主要结合在纤维表面。结果表明，赖氨酰氧化酶在胶原蛋白纤维形成的早期阶段启动交联形成。
