Rate of helix formation by intracellular procollagen and protocollagen. Evidence for a role for disulfide bonds. Academic Article uri icon


  • Matrix-free cells from embryonic tendons were incubated under conditions in which they synthesized and accumulated protocollagen, the unhydroxylated form of procollagen, which is non-helical at 37. Limited digestion with pepsin demonstrated that when the accumulated protocollagen was hydroxylated intracellularly to procollagen, or when the cells were cooled below the Tm of protocollagen, the protein became triple-helical in about 5 min, or in a fraction of the time required for isolated chains to become helical. When disulfide bonds in the NH2-terminal extensions of protocollagen were reduced by treating the cells with dithiothreitol, the rate of helix formation was markedly decreased. The results demonstrated that the NH2-terminal extensions found in protocollagen and procollagen play an important role in formation of the triple-helix during biosynthesis. 1973.

published proceedings

  • Biochem Biophys Res Commun

altmetric score

  • 3

author list (cited authors)

  • Uitto, J., & Prockop, D. J.

citation count

  • 51

complete list of authors

  • Uitto, J||Prockop, DJ

publication date

  • January 1973