Differences between proline and lysine hydroxylations in their inhibition by zinc or by ascorbate deficiency during collagen synthesis in various cell types
- 1 May 1981
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - General Subjects
- Vol. 674 (3) , 336-344
- https://doi.org/10.1016/0304-4165(81)90364-0
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Effects of divalent cations on collagen biosynthesis in isolated chick embryo tendon cellsBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1980
- Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous proteinBiochemical Journal, 1980
- Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanismBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspectsBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- The Biosynthesis of Collagen and Its DisordersNew England Journal of Medicine, 1979
- The Biosynthesis of Collagen and Its DisordersNew England Journal of Medicine, 1979
- Collagen GlycosyltransferasesPublished by Elsevier ,1979
- Mechanism of the Prolyl Hydroxylase ReactionEuropean Journal of Biochemistry, 1977
- Mechanism of the Prolyl Hydroxylase ReactionEuropean Journal of Biochemistry, 1977
- Lysyl hydroxylase. Further purification and characterization of the enzume from chick embryos and chick embryo cartilageBiochimica et Biophysica Acta (BBA) - Enzymology, 1976