Bächinger H P, Doege K J, Petschek J P, Fessler L I, Fessler J H
J Biol Chem. 1982 Dec 25;257(24):14590-2.
Chick embryo procollagen V, procollagen I, and pC-collagen I were sprayed, rotary shadowed, and compared electronmicroscopically with mouse procollagen IV and Drosophila procollagen produced by cell cultures and prepared in the same way. All the molecules appeared as threads and had a prominent knob protrusion at one end. For procollagen I and pC-collagen I this must correspond to the carboxyl propeptides, and most likely corresponds to the similarly sized carboxyl propeptides of procollagen IV. Procollagen V appeared as a thread of nearly the same length as procollagen I but with substantial knobs at both ends, corresponding to its known propeptides. The length of procollagen V and the known, successive processing of its propeptides make procollagen V more similar to the interstitial collagens than to the basement membrane procollagen IV, which is 1.4 times as long and has so far been found not to be processed. Drosophila procollagen resembles procollagen IV in length and appearance.
将鸡胚原胶原蛋白V、原胶原蛋白I和前胶原C-胶原蛋白I进行喷雾、旋转投影，并与通过细胞培养以相同方式制备的小鼠原胶原蛋白IV和果蝇原胶原蛋白进行电子显微镜比较。所有分子均呈丝状，一端有一个明显的球状突起。对于原胶原蛋白I和前胶原C-胶原蛋白I，这必定对应于羧基前肽，很可能也对应于原胶原蛋白IV中大小相似的羧基前肽。原胶原蛋白V呈现为一条与原胶原蛋白I长度几乎相同的丝状，但两端都有明显的球状结构，这与其已知的前肽相对应。原胶原蛋白V的长度以及其前肽已知的连续加工过程，使得原胶原蛋白V与间质胶原蛋白的相似性高于基底膜原胶原蛋白IV，后者的长度是前者的1.4倍，且迄今为止尚未发现其会被加工。果蝇原胶原蛋白在长度和外观上与原胶原蛋白IV相似。
