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- Evans W. C., Richard W., Handley C., Happold F. C. The tryptophanase-indole reaction: Some observations on the production of tryptophanase by Esch. coli; in particular the effect of the presence of glucose and amino acids on the formation of tryptophanase. Biochem J. 1941 Jan;35(1-2):207–212. doi: 10.1042/bj0350207. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fildes P. The production of indole by suspensions of Bact. coli. Biochem J. 1938 Sep;32(9):1600–1606. doi: 10.1042/bj0321600. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Happold F. C., Hoyle L. The quantitative determination of indole in bacterial cultures. Biochem J. 1934;28(4):1171–1173. doi: 10.1042/bj0281171. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kendal L. P., Stickland L. H. Studies in glycolysis: The first stages of glycolysis in muscle extracts. Biochem J. 1938 Mar;32(3):572–584. doi: 10.1042/bj0320572. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Needham J., Lehmann H. Intermediary carbohydrate metabolism in embryonic life: Phosphorylation cycles. VI. Glucolysis without phosphorylation. VII. Experiments on the nature of non-phosphorylating glucolysis. Biochem J. 1937 Jul;31(7):1210–1254. doi: 10.1042/bj0311210. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stickland L. H. The inhibition of glucolysis by glyceraldehyde. Biochem J. 1941 Sep;35(8-9):859–871. doi: 10.1042/bj0350859. [DOI] [PMC free article] [PubMed] [Google Scholar]