Partial Hydroxylation of Certain Lysines In Collagen
- 23 August 1968
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 161 (3843), 796-798
- https://doi.org/10.1126/science.161.3843.796
Abstract
Peptides derived from the al chain of collagen have been isolated in small amounts and have been shown to differ from ones found in expected amounts only by substitution of hydroxylysine for lysine. This observation indicates that hydroxylation of these lysines by protocollagen hydroxylase has been effected to a very minor extent.Keywords
This publication has 15 references indexed in Scilit:
- Independence of collagen hydroxylation on the conformational state of the precursor substrateBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Isolation and Characterization of the Cyanogen Bromide Peptides from the α1 Chain of Rat Skin Collagen*Biochemistry, 1967
- Effect of cycloheximide on collagen biosynthesis as evidence for a post-ribosomal site for the hydroxylation of prolineBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1967
- Comparative Sequence Studies of Rat Skin and Tendon Collagen. I. Evidence for Incomplete Hydroxylation of Individual Prolyl Residues in the Normal Proteins*Biochemistry, 1967
- Formation of Hydroxyproline in CollagenScience, 1966
- Deuterated Organisms: Cultivation and UsesScience, 1966
- Association and Dissociation of Phycocyanin and the Effects of Deuterium Substitution on the Processes*Biochemistry, 1965
- Hydrogen Exchange at Carbon-Hydrogen Sites during Acid or Alkaline Treatment of ProteinsBiochemistry, 1964
- Mass cultivation of algae in pure heavy waterBiotechnology & Bioengineering, 1962
- Isolation of Fully Deuterated Metabolites from Scenedesmus obliquus Grown in Deuterium OxideJournal of Pharmaceutical Sciences, 1961