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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- HARLEY-MASON J. Mechanism of tryptophane biogenesis and decomposition. Experientia. 1954 Mar 15;10(3):134–135. doi: 10.1007/BF02158517. [DOI] [PubMed] [Google Scholar]
- LERNER P., YANOFSKY C. An immunological study of mutants of Escherichia coli lacking the enzyme tryptophan synthetase. J Bacteriol. 1957 Oct;74(4):494–501. doi: 10.1128/jb.74.4.494-501.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Richards F. M. ON THE ENZYMIC ACTIVITY OF SUBTILISIN-MODIFIED RIBONUCLEASE. Proc Natl Acad Sci U S A. 1958 Feb;44(2):162–166. doi: 10.1073/pnas.44.2.162. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TATUM E. L., SHEMIN D. Mechanism of tryptophan synthesis in Neurospora. J Biol Chem. 1954 Aug;209(2):671–675. [PubMed] [Google Scholar]
- YANOFSKY C. Enzymatic studies with a series of tryptophan auxotrophs of Escherichia coli. J Biol Chem. 1957 Feb;224(2):783–792. [PubMed] [Google Scholar]
- YANOFSKY C., RACHMELER M. The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim Biophys Acta. 1958 Jun;28(3):640–641. doi: 10.1016/0006-3002(58)90533-x. [DOI] [PubMed] [Google Scholar]
- YANOFSKY C. The absence of a tryptophan-niacin relationship in Escherichia coli and Bacillus subtilis. J Bacteriol. 1954 Nov;68(5):577–584. doi: 10.1128/jb.68.5.577-584.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yanofsky C., Stadler J. THE ENZYMATIC ACTIVITY ASSOCIATED WITH THE PROTEIN IMMUNOLOGICALLY RELATED TO TRYPTOPHAN SYNTHETASE. Proc Natl Acad Sci U S A. 1958 Mar;44(3):245–253. doi: 10.1073/pnas.44.3.245. [DOI] [PMC free article] [PubMed] [Google Scholar]