Mallinger R, Schmut O
Institut für Mikromorphologie und Elektronenmikroskopie, Universität Wien, Vienna, Austria.
J Ultrastruct Mol Struct Res. 1988 Jan;98(1):11-8. doi: 10.1016/s0889-1605(88)80930-3.
Segment long-spacing collagen (SLS) can be precipitated from solutions of collagen using ATP as the inducing agent. Dimeric SLS aggregates have been observed in addition to monomeric SLS. We have compared collagen types I, II, III, and V with respect to their ability to form dimeric SLS in vitro. These collagen types were isolated from bovine tissues and characterized by polyacrylamide slab gel electrophoresis of the respective alpha-chains. Only monomeric SLS can be detected in preparations of collagen types I and III. Dimeric SLS, on the other hand, accounts for the majority of the crystallites seen in preparations of collagen types II and V. Dimeric SLS from both collagen types II and V reveal overlap zones at the carboxy-terminal ends of the collagen molecules. However, dimeric SLS from collagen types II and V differ with respect to their overlap distances. Significant portions of the triple helical domains of collagen molecules are occupied by the overlap region of dimeric SLS from type II collagen. On the other hand, dimeric SLS from type V collagen is composed of molecules overlapping only at their short nonhelical telopeptides. It is concluded that the ability of collagen molecules to aggregate into dimeric SLS under defined experimental conditions is collagen type dependent.
使用ATP作为诱导剂,可以从胶原蛋白溶液中沉淀出长间距胶原(SLS)。除了单体SLS外,还观察到二聚体SLS聚集体。我们比较了I型、II型、III型和V型胶原蛋白在体外形成二聚体SLS的能力。这些胶原蛋白类型从牛组织中分离出来,并通过各自α链的聚丙烯酰胺平板凝胶电泳进行表征。在I型和III型胶原蛋白制剂中只能检测到单体SLS。另一方面,二聚体SLS在II型和V型胶原蛋白制剂中所见的微晶中占大多数。来自II型和V型胶原蛋白的二聚体SLS在胶原蛋白分子的羧基末端显示出重叠区域。然而,来自II型和V型胶原蛋白的二聚体SLS在其重叠距离方面有所不同。II型胶原蛋白二聚体SLS的重叠区域占据了胶原蛋白分子三螺旋结构域的很大一部分。另一方面,V型胶原蛋白的二聚体SLS由仅在其短的非螺旋端肽处重叠的分子组成。结论是,在确定的实验条件下,胶原蛋白分子聚集成二聚体SLS的能力取决于胶原蛋白类型。