title: Collagen polypeptides: normal release from polysomes in the absence of proline hydroxylation.
abstract: It is not necessary that proline be hydroxylated for the completion and release of nascent collagen chains from polysomes. Hydroxylation of collagen proline in vivo normally takes place predominantly on nascent polypeptides; however, in the presence of an inhibitor of hydroxylation, unhydroxylated chains are released. These chains may subsequently be hydroxylated when the inhibition is removed. The results clarify a controversy over the site of proline hydroxylation.
mesh_terms: D000818:Animals; D002499:Centrifugation, Density Gradient; D002614:Chelating Agents / Q000494:pharmacology; D003094:Collagen / Q000096:biosynthesis*; D006909:Hydroxyproline / Q000378:metabolism*; D066298:In Vitro Techniques; D051379:Mice; D010452:Peptide Biosynthesis; D010455:Peptides / Q000032:analysis; D011392:Proline / Q000378:metabolism*; D011725:Pyridines / Q000494:pharmacology; D012270:Ribosomes / Q000378:metabolism*; D014316:Tritium
chemical_list: D002614:Chelating Agents; D010455:Peptides; D011725:Pyridines; D014316:Tritium; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline