Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002642:Chick Embryo; D008854:Microscopy, Electron; D010455:Peptides / Q000032:analysis; D011347:Procollagen / Q000032:analysis* / Q000302:isolation & purification
D010455:Peptides; D011347:Procollagen