Fitzsimmons C M, Cawston T E, Barnes M J
Thromb Haemost. 1986 Aug 20;56(1):95-9.
In this study, the ability of peptides, obtained by fragmentation of the collagen type I molecule, to induce platelet aggregation has been examined. In order to satisfy requirements for tertiary and quaternary structure, peptides were first renatured (where necessary) to restore triple-helical configuration and then polymerised. Fragmentation with mammalian collagenase indicated the presence of platelet-reactive sites in both the N-terminal three-quarter and C-terminal one quarter fragment of the collagen molecule. Cleavage with cyanogen bromide indicated the presence in the constituent alpha 1(I)-chain of at least four platelet-reactive sites. Our results suggest a relatively wide distribution of platelet-binding sites situated throughout the length of the collagen (type I) molecule, each probably of relatively low affinity and low structural specificity, at least in terms of amino acid sequence, and probably of a similar nature to those that might be expected to exist in any collagen-like species.
在本研究中，对通过I型胶原分子片段化获得的肽诱导血小板聚集的能力进行了检测。为满足三级和四级结构的要求，首先对肽进行复性（必要时）以恢复三螺旋构型，然后进行聚合。用哺乳动物胶原酶进行片段化表明，胶原分子的N端四分之三片段和C端四分之一片段中均存在血小板反应位点。用溴化氰切割表明，在组成α1（I）链中至少存在四个血小板反应位点。我们的结果表明，血小板结合位点在整个胶原（I型）分子长度上分布相对广泛，至少就氨基酸序列而言，每个位点的亲和力可能相对较低且结构特异性较低，并且其性质可能与预期存在于任何类胶原物种中的位点相似。
