Affinity Column Purification of Protocollagen Proline Hydroxylase from Chick Embryos and Further Characterization of the Enzyme
Open Access
- 1 February 1973
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 248 (4) , 1175-1182
- https://doi.org/10.1016/s0021-9258(19)44278-6
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Partial purification and characterization of protocollagen lysine hydroxylase from chick embryosBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Partial purification and properties of collagen lysine hydroxylase from chick embryosBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of α-ketoglutarateBiochemistry, 1972
- The substrate recognition site of collagen proline hydroxylase: The hydroxylation of -X-Pro-Gly- sequences in bradykinin analogs and other peptidesArchives of Biochemistry and Biophysics, 1971
- Protocollagen proline hydroxylase: Molecular weight, subunits and isoelectric pointBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Isolation and partial characterization of highly purified protocollagen proline hydroxylaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- Synthetic polypeptides as substrates and inhibitors of collagen proline hydroxylaseArchives of Biochemistry and Biophysics, 1968
- Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins in concentrated aqueous cesium chloride and guanidine hydrochlorideJournal of the American Chemical Society, 1967
- Enzymatic Synthesis of Hydroxyproline by the Hydroxylation of Poly(L-prolyl-glycyl-L-prolyl)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1967
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965