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May 1, 1984Journal of Biological ChemistryOpen Access

Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase.

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Authors

RMRaili MyllyläAcademy of Medical SciencesKMKari MajamaaOulu University HospitalVGVolkmar GünzlerStowers Institute for Medical Research

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Myllylä et al. (1984) studied this question.

synapsesocial.com/papers/6a714376f44fa9f079df0c0dhttps://doi.org/10.1016/s0021-9258(18)91023-9
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Affinity Column Purification of Protocollagen Proline Hydroxylase from Chick Embryos and Further Characterization of the Enzyme1973 · 168 citations
  2. 2An Affinity‐Column Procedure Using Poly( l ‐proline) for the Purification of Prolyl Hydroxylase1975 · 167 citations
  3. 3Prolyl hydroxylase half reaction: peptidyl prolyl-independent decarboxylation of alpha-ketoglutarate.1978 · 62 citations
  4. 4Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarate1972 · 82 citations