The primary structure of Lactobacillus casei thymidylate synthetase. III. The use of 2-(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine and limited tryptic peptides to establish the complete amino acid sequence of the enzyme.
Open Access
- 1 February 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (4) , 1301-1304
- https://doi.org/10.1016/s0021-9258(17)34202-3
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
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- Amino acid sequence at the FdUMP binding site of thymidylate synthetase.Proceedings of the National Academy of Sciences, 1976
- Thymidylate synthetase: Studies on the peptide containing covalently bound 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolateBiochemical and Biophysical Research Communications, 1976
- The Carboxypeptidase-dependent Inactivation of Thymidylate SynthetaseJournal of Biological Chemistry, 1974
- [34] Modification of tryptophan with BNPS-skatole (2-(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine)Published by Elsevier ,1972
- Cleavage of Histidyl Peptide Bonds by N-BromosuccinimideJournal of the American Chemical Society, 1963