Evidence for an exceptionally reactive arginyl residue at the binding site for carbamyl phosphate in bovine ornithine transcarbamylase.
Open Access
- 31 July 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (15) , 7301-7305
- https://doi.org/10.1016/s0021-9258(20)79703-6
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Ornithine transcarbamylases. Ordering of S-cyano peptides and location of characteristically reactive cysteinyl residues within the sequence.Journal of Biological Chemistry, 1980
- Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5'-phosphate.Journal of Biological Chemistry, 1977
- An essential residue at the active site of aspartate transcarbamylase.Journal of Biological Chemistry, 1976
- Essential arginyl residue at the nucleotide binding site of creatine kinaseBiochemistry, 1975
- Modification of Arginyl Residues in Porcine Carboxypeptidase BEuropean Journal of Biochemistry, 1975
- Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residuesJournal of Biological Chemistry, 1975
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Ornithine Transcarbamylase from Streptococcus faecalis and Bovine LiverPublished by Elsevier ,1972
- The Reaction of Phenylglyoxal with Arginine Residues in ProteinsJournal of Biological Chemistry, 1968
- A sensitive method for serum ornithine carbamyltransferase determinationClinica Chimica Acta; International Journal of Clinical Chemistry, 1966