Biosynthesis of type I procollagen. Characterization of the distribution of chain sizes and extent of hydroxylation of polysome-associated pro-alpha-chains.

@article{Kirk1987BiosynthesisOT,
  title={Biosynthesis of type I procollagen. Characterization of the distribution of chain sizes and extent of hydroxylation of polysome-associated pro-alpha-chains.},
  author={T Z Kirk and James S Evans and Arthur Veis},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 12},
  pages={5540-5}
}
[3H]Proline-labeled nascent procollagen chains were isolated from chick tendon polysome preparations as peptidyl-tRNA complexes by ion exchange chromatography. Proline hydroxylation of the nascent chains was at least 40% complete, based on radioactive hydroxyproline/proline ratios. These data provide the first direct evidence that hydroxylation of procollagen proline residues does occur on nascent chains. The electrophoretic profiles of [3H]proline-labeled nascent chains and of unlabeled… CONTINUE READING

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Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
Proline hydroxylation of the nascent chains was at least 40% complete , based on radioactive hydroxyproline / proline ratios .
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