In Vitro Enzymatic Hydroxylation of Prolyl Residues in the α1-CB2 Fragment of Rat Collagen
Open Access
- 1 July 1971
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 246 (13) , 4138-4142
- https://doi.org/10.1016/s0021-9258(18)62064-2
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Hydroxylation of proline residues in collagen nascent chainsArchives of Biochemistry and Biophysics, 1970
- Structure of α1-CB8, a large cyanogen bromide produced fragment from the α1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptidesBiochemistry, 1970
- Hydroxylation of proline and lysine in protocollagen involves two separate enzymatic sitesBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- Substrate specificity of collagen proline hydroxylase: Hydroxylation of a specific proline residue in bradykininArchives of Biochemistry and Biophysics, 1969
- Specificities of protocollagen hydroxylases from different sourcesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- Hydroxylation of poly(l-prolyl-l-prolylglycyl) of defined molecular weights by protocollagen proline hydroxylaseFEBS Letters, 1969
- Synthetic polypeptides as substrates and inhibitors of collagen proline hydroxylaseArchives of Biochemistry and Biophysics, 1968
- Independence of collagen hydroxylation on the conformational state of the precursor substrateBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Kinetic patterns of protocollagen hydroxylase and further studies on the polypeptide substrateBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- Relationship between the positioning of pyrrolidine residues and the stability of collagenJournal of Molecular Biology, 1966