Hoffmann H P, Olsen B R, Chen H T, Prockop D J
Proc Natl Acad Sci U S A. 1976 Dec;73(12):4304-8. doi: 10.1073/pnas.73.12.4304.
Type I procollagen secreted by matrix-free cells from chick embryo tendons was purified by DEAE-cellulose chromatography. Electron microscopy of segment-long-spacing aggregates of the procollagen demonstrated the presence of both NH2-terminal and COOH-terminal extensions not found in collagen. The procollagen was digested with bacterial collagenase and the COOH-terminal fragments were isolated by gel filtration and polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Analysis of tryptic peptides demonstrated that the COOH-terminal extensions on the pro alpha 1 and pro alpha 2 chains had different primary structures.
通过DEAE - 纤维素色谱法对来自鸡胚肌腱的无基质细胞分泌的I型前胶原进行了纯化。对前胶原的片段长间距聚集体进行电子显微镜观察，结果表明存在胶原中未发现的NH2末端和COOH末端延伸。用细菌胶原酶消化前胶原，并通过凝胶过滤和十二烷基硫酸钠聚丙烯酰胺凝胶电泳分离COOH末端片段。对胰蛋白酶肽段的分析表明，前α1链和前α2链上的COOH末端延伸具有不同的一级结构。
