Full text
PDF












Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BECK W. S., FLAVIN M., OCHOA S. Metabolism of propionic acid in animal tissues. III. Formation of succinate. J Biol Chem. 1957 Dec;229(2):997–1010. [PubMed] [Google Scholar]
- DE LEY J., SCHEL J. Studies on the metabolism of Acetobacter peroxydans. II. The enzymic mechanism of lactate metabolism. Biochim Biophys Acta. 1959 Sep;35:154–165. doi: 10.1016/0006-3002(59)90344-0. [DOI] [PubMed] [Google Scholar]
- DENNIS D., KAPLAN N. O. D- and L-lactic acid dehydrogenases in Lactobacillus plantarum. J Biol Chem. 1960 Mar;235:810–818. [PubMed] [Google Scholar]
- ELLIOTT W. H. A new threonine metabolite. Biochim Biophys Acta. 1958 Aug;29(2):446–447. doi: 10.1016/0006-3002(58)90215-4. [DOI] [PubMed] [Google Scholar]
- ELLIOTT W. H. Amino-acetone; its isolation and role in metabolism. Nature. 1959 Apr 11;183(4667):1051–1052. doi: 10.1038/1831051a0. [DOI] [PubMed] [Google Scholar]
- ELLIOTT W. H. Aminoacetone formation by Staphylococcus aureus. Biochem J. 1960 Mar;74:478–485. doi: 10.1042/bj0740478. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ELLIOTT W. H. The estimation of aminoacetone and 5-aminolaevulic acid. Biochem J. 1960 Jan;74:90–94. doi: 10.1042/bj0740090. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GOLDSTEIN L., KNOX W. E., BEHRMAN E. J. Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver. J Biol Chem. 1962 Sep;237:2855–2860. [PubMed] [Google Scholar]
- GREGOLIN C., SINGER T. P. The lactic dehydrogenase of yeast. III. D(-)Lactic cytochrome c reductase, a zinc-flavoprotein from aerobic yeast. Biochim Biophys Acta. 1963 Feb 12;67:201–218. doi: 10.1016/0006-3002(63)91818-3. [DOI] [PubMed] [Google Scholar]
- Green M. L. The activation of L-threonine dehydrogenase by potassium ions. Biochem J. 1964 Sep;92(3):550–555. doi: 10.1042/bj0920550. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HARTSHORNE D., GREENBERG D. M. STUDIES ON LIVER THREONINE DEHYDROGENASE. Arch Biochem Biophys. 1964 Apr;105:173–178. doi: 10.1016/0003-9861(64)90250-4. [DOI] [PubMed] [Google Scholar]
- Hopkins F. G., Morgan E. J. Studies on glyoxalase: 1. A new factor. Biochem J. 1948;42(1):23–27. [PMC free article] [PubMed] [Google Scholar]
- KARASEK M. A., GREENBERG D. M. Studies on the properties of threonine aldolases. J Biol Chem. 1957 Jul;227(1):191–205. [PubMed] [Google Scholar]
- KELLY C. D., LAYNE S. Bacteria found in the air over Canada and the American Arctic. Can J Microbiol. 1957 Apr;3(3):447–455. doi: 10.1139/m57-047. [DOI] [PubMed] [Google Scholar]
- KORKES S., DEL CAMPILLO A., GUNSALAS I. C., OCHOA S. Enzymatic synthesis of citric acid. IV. Pyruvate as acetyl donor. J Biol Chem. 1951 Dec;193(2):721–735. [PubMed] [Google Scholar]
- LEHNINGER A. L., SUDDUTH H. C., WISE J. B. D-beta-Hydroxybutyric dehydrogenase of muitochondria. J Biol Chem. 1960 Aug;235:2450–2455. [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]
- MAUZERALL D., GRANICK S. The occurrence and determination of delta-amino-levulinic acid and porphobilinogen in urine. J Biol Chem. 1956 Mar;219(1):435–446. [PubMed] [Google Scholar]
- NEUBERGER A. Aspects of the metabolism of glycine and of porphyrins. Biochem J. 1961 Jan;78:1–10. doi: 10.1042/bj0780001. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NEUBERGER A., TAIT G. H. Production of aminoacetone by Rhodopseudomonas spheroides. Biochem J. 1962 Aug;84:317–328. doi: 10.1042/bj0840317. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NEUBERGER A., TAIT G. H. The enzymic conversion of threonine to aminoacetone. Biochim Biophys Acta. 1960 Jun 17;41:164–165. doi: 10.1016/0006-3002(60)90388-7. [DOI] [PubMed] [Google Scholar]
- NISHIMURA J. S., GREENBERG D. M. Purification and properties of L-threonine dehydrase of sheep liver. J Biol Chem. 1961 Oct;236:2684–2691. [PubMed] [Google Scholar]
- NORDLIE R. C., FROMM H. J. Ribitol dehydrogenase. II. Studies on the reaction mechanism. J Biol Chem. 1959 Oct;234:2523–2531. [PubMed] [Google Scholar]
- NYGAARD A. P. D(-)-Lactic cytochrome c reductase, a flavo-protein from yeast. J Biol Chem. 1961 Mar;236:920–925. [PubMed] [Google Scholar]
- TUBBS P. K., GREVILLE G. D. The oxidation of D-alpha-hydroxy acids in animal tissues. Biochem J. 1961 Oct;81:104–114. doi: 10.1042/bj0810104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TUCKER R. G. The oxidation of tricarboxylic acid cycle intermediates by a strain of Corynebacterium erythrogenes. J Gen Microbiol. 1960 Oct;23:267–282. doi: 10.1099/00221287-23-2-267. [DOI] [PubMed] [Google Scholar]
- UMBARGER H. E., BROWN B. Threonine deamination in Escherichia coli. I. D- and L-threonine deaminase activities of cell-free extracts. J Bacteriol. 1956 Apr;71(4):443–449. doi: 10.1128/jb.71.4.443-449.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
- URATA G., GRANICK S. Aminoacetone formation and decomposition in liver. Biochem Biophys Res Commun. 1961 Feb 24;4:96–100. doi: 10.1016/0006-291x(61)90354-0. [DOI] [PubMed] [Google Scholar]
- URATA G., GRANICK S. Biosynthesis of alpha-aminoketones and the metabolism of aminoacetone. J Biol Chem. 1963 Feb;238:811–820. [PubMed] [Google Scholar]
- WALTER C., FRIEDEN E. THE PREVALENCE AND SIGNIFICANCE OF THE PRODUCT INHIBITION OF ENZYMES. Adv Enzymol Relat Areas Mol Biol. 1963;25:167–274. doi: 10.1002/9780470122709.ch4. [DOI] [PubMed] [Google Scholar]
- WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WOOD W. A., GUNSALUS I. C. D-Alanine formation; a racemase in Streptococcus faecalis. J Biol Chem. 1951 May;190(1):403–416. [PubMed] [Google Scholar]
- von HOFSTEN, FALKBRING S. O. A simple arrangement for the concentration of protein solutions. Anal Biochem. 1960 Dec 10;1:436–439. doi: 10.1016/0003-2697(60)90042-7. [DOI] [PubMed] [Google Scholar]