Mikhaĭlov A N, Titova E F, Belavtseva E M
Biofizika. 1979 May-Jun;24(3):438-41.
Comparative electron microscopic investigation of submolecular structure formation of native collagen molecules and denaturated collagen peptides in tropocollagen and gelatin gels was carried out. Submolecular terminal structures were similar. Fibrils exist with cross striation region of 64--70 nm. In spite of this the intermediate steps in the formation of both structures differ. In case of collagen the bundle of parallel microfibrils forms the thick fibrils. In case of gelatin the aggregates of spherical anisotropic particles form the fibrils of gelatin gels.
对原胶原蛋白和明胶凝胶中天然胶原分子和变性胶原肽的亚分子结构形成进行了比较电子显微镜研究。亚分子末端结构相似。存在横纹区域为64 - 70纳米的原纤维。尽管如此，两种结构形成的中间步骤有所不同。对于胶原蛋白，平行微纤维束形成粗原纤维。对于明胶，球形各向异性颗粒的聚集体形成明胶凝胶的原纤维。
