Biosynthesis of cartilage procollagen. Influence of chain association and hydroxylation of prolyl residues on the folding of the polypeptides into the triple-helical conformation

Biochemistry. 1974 Oct 22;13(22):4586-91. doi: 10.1021/bi00719a018.
No abstract available

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Binding Sites
  • Carbon Radioisotopes
  • Cartilage / metabolism
  • Chick Embryo
  • Chromatography, Gel
  • Collagen* / biosynthesis
  • Disulfides / analysis
  • Electrophoresis, Polyacrylamide Gel
  • Hydroxyproline / biosynthesis
  • Hypoxia / metabolism
  • Iodoacetates
  • Isotope Labeling
  • Kinetics
  • Microbial Collagenase
  • Proline / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Precursors* / biosynthesis
  • Time Factors
  • Trypsin

Substances

  • Carbon Radioisotopes
  • Disulfides
  • Iodoacetates
  • Protein Precursors
  • Collagen
  • Proline
  • Trypsin
  • Microbial Collagenase
  • Hydroxyproline