Ghosh S K, Mitra H P
Biochim Biophys Acta. 1975 Oct 20;405(2):340-6. doi: 10.1016/0005-2795(75)90099-9.
Collagen fibres from rat tail tendon suspended in small pieces in a solution (pH 7.8) containing 0.5 M CaCl2 were treated with purified bovine trypsin at 20 degrees C for 20 h. After the enzyme treatment collagen from this solution was precipitated out and reconstituted in vitro into native-type fibrils. The banding pattern in these reconstituted fibrils was found to be oblique. This is comparable to that observed recently in fibrils reconstituted from cartilage collagen. On the other hand, normal transverse banding pattern was observed in the fibrils reconstituted in vitro from collagen solution of rat tail tendon which was not pre-treated with trypsin. No significant change was, however, observed in the segment long spacing fibrils precipitated from the enzyme-treated collagen solution. It is possible that the enzyme might affect the mode of organization of tropocollagen molecules during in vitro fibrillogenesis into native-type fibrils either by interacting with the "telopeptide" regions or with the non-collagenous components associated with the native protein and this could probably result into the formation of fibrils with oblique banding pattern.
将大鼠尾腱的胶原纤维切成小块，悬浮于含有0.5M氯化钙的溶液（pH7.8）中，在20℃下用纯化的牛胰蛋白酶处理20小时。酶处理后，从该溶液中沉淀出胶原，并在体外重构成天然型原纤维。发现这些重构原纤维中的条纹模式是倾斜的。这与最近在由软骨胶原重构的原纤维中观察到的情况相当。另一方面，在未用胰蛋白酶预处理的大鼠尾腱胶原溶液体外重构的原纤维中观察到正常的横向条纹模式。然而，从酶处理的胶原溶液中沉淀出的段长间距原纤维没有观察到明显变化。酶可能通过与“端肽”区域或与天然蛋白质相关的非胶原成分相互作用，在体外原纤维形成天然型原纤维的过程中影响原胶原蛋白分子的组装方式，这可能导致形成具有倾斜条纹模式的原纤维。
