Hydroxylation of (Pro-Pro-Gly)5and (Pro-Pro-Gly)10by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00627a014
Reference39 articles.
1. Titration and Melting Curves of the Collagen-like Triple Helices Formed from (Pro-Pro-Gly)10 in Aqueous Solution
2. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
3. Affinity Column Purification of Protocollagen Proline Hydroxylase from Chick Embryos and Further Characterization of the Enzyme
4. Purification of carbon-14-labeled protocollagen and its hydroxylation by prolyl-hydroxylase
5. Berg, R. A., and Prockop, D. J. (1976), inThe Methodology of Connective Tissue Research, Hall, D. A., Ed.Oxford, Joynson-Bruvvers Ltd., p187.
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