Adachi E, Hayashi T
Coll Relat Res. 1985 Jun;5(3):225-32. doi: 10.1016/s0174-173x(85)80012-1.
Type V collagen was isolated from human placenta by limited pepsin treatment and purified by salt fractionation. A solution of type V collagen was dialyzed at 4 degrees C against phosphate-buffered saline or against 0.02 M Na2HPO4. Aggregates formed under these in vitro conditions from a pure type V collagen solution were examined by electron microscopy. The aggregates were fine flexible fibrils. The fibrils formed during incubation at 25 degrees C were of relatively uniform diameter, 34.8 +/- 9.1 nm and did not show an axial banding pattern. When the specimen was incubated at 37 degrees C, the fibrils were of slightly larger diameter, 38.2 +/- 9.1 nm and almost all the fibrils had the axial repeat pattern of 67 nm. The ability of type V collagen to form banding fibrils is discussed in relation in the localization of the collagen in tissues.
通过有限的胃蛋白酶处理从人胎盘中分离出V型胶原蛋白，并通过盐分级分离进行纯化。将V型胶原蛋白溶液在4℃下对磷酸盐缓冲盐水或0.02M Na2HPO4进行透析。通过电子显微镜检查在这些体外条件下由纯V型胶原蛋白溶液形成的聚集体。聚集体是细的柔性纤维。在25℃孵育期间形成的纤维直径相对均匀，为34.8±9.1nm，并且没有显示出轴向条纹图案。当样品在37℃孵育时，纤维直径稍大，为38.2±9.1nm，并且几乎所有纤维都具有67nm的轴向重复图案。讨论了V型胶原蛋白形成条纹纤维的能力与胶原蛋白在组织中的定位的关系。
