Procollagen: intermediate forms containing several types of peptide chains and non-collagen peptide extensions at NH2 and COOH ends.
A population of procollagen molecules has been isolated from the culture medium of a clonal line of calf dermatosparactic cells and shown to have the amino-acid composition, physical properties, and molecular structure consistent with collagen precursors. Although this procollagen population shares immunologic determinants with the procollagen obtained from dermatosparactic skin, it differs from the latter in aminoacid composition, in subunit properties, and by its content of both amino and carboxyl terminal non-collagen peptide appendages. We propose that the cell culture procollagen contains earlier biosynthetic forms of dermatosparactic procollagen.
D002250:Carbon Radioisotopes; D002999:Clone Cells; D003094:Collagen / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D003012:Microbial Collagenase; D008854:Microscopy, Electron; D010454:Peptide Termination Factors; D010455:Peptides / Q000032:analysis; D011392:Proline / Q000378:metabolism; D011498:Protein Precursors / Q000032:analysis* / Q000096:biosynthesis; D012967:Sodium Dodecyl Sulfate; D014316:Tritium
D002250:Carbon Radioisotopes; D010454:Peptide Termination Factors; D010455:Peptides; D011498:Protein Precursors; D014316:Tritium; D012967:Sodium Dodecyl Sulfate; D003094:Collagen; D011392:Proline; D003012:Microbial Collagenase