Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex.

@article{Risteli1977Prolyl3P,
  title={Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex.},
  author={J. Risteli and K. Tryggvason and K. Kivirikko},
  journal={European journal of biochemistry},
  year={1977},
  volume={73 2},
  pages={
          485-92
        }
}
The formation of 3-hydroxyproline was studied with crude rat kidney cortex extract as a source of enzyme and chick embryo tendon protocollagen and procollagen or cartilage protocollagen as a substrate. Synthesis of 3-hydroxyproline was observed with all these substrates and the formation of 3-hydroxyproline ranged up to seven residues per pro-alpha-chain. The highest rate of 3-hydroxylation took place at 20 degrees C and the reaction required Fe2+, O2,2-oxoglutarate and ascorbate. The formation… Expand
A rapid assay for prolyl 3-hydroxylase activity.
Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.
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