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. 1960 May;75(2):401–408. doi: 10.1042/bj0750401

Glutamic-aspartic transaminase of Dolichos lablab: participation by iron as a cofactor

M V Patwardhan 1
PMCID: PMC1204438  PMID: 14430956

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BROWN E. G. Evidence for the involvement of ferrous iron in the biosynthesis of delta-aminolaevulic acid by chicken erythrocyte preparations. Nature. 1958 Aug 2;182(4631):313–315. doi: 10.1038/182313b0. [DOI] [PubMed] [Google Scholar]
  2. CRUICKSHANK D. H., ISHERWOOD F. A. Glutamic-alanine and glutamic-aspartic transaminases of wheat germ. Biochem J. 1958 Jun;69(2):189–195. doi: 10.1042/bj0690189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. EGGLESTON L. V. Effects of cations on amino acid decarboxylases. Biochem J. 1958 Mar;68(3):557–560. doi: 10.1042/bj0680557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. HAPPOLD F. C., STRUYVENBERG A. The activation of tryptophanase apo-enzyme by potassium, ammonium and rubidium ions. Biochem J. 1954 Nov;58(3):379–382. doi: 10.1042/bj0580379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HAPPOLD F. C., TURNER J. M. Effect of magnesium ions on heart-muscle transaminase. Nature. 1957 Jan 19;179(4551):155–156. doi: 10.1038/179155a0. [DOI] [PubMed] [Google Scholar]
  6. ISHERWOOD F. A., CRUICKSHANK D. H. Chromatographic separation and analysis of mixtures of pyruvic, oxalacetic and alpha-ketoglutaric acids. Nature. 1954 Jan 16;173(4394):121–122. doi: 10.1038/173121a0. [DOI] [PubMed] [Google Scholar]
  7. JAKOBY W. B., BONNER D. M. Kynureninase from Neurospora: purification and properties. J Biol Chem. 1953 Dec;205(2):699–707. [PubMed] [Google Scholar]
  8. Krebs H. A. The effect of inorganic salts on the ketone decomposition of oxaloacetic acid. Biochem J. 1942 Apr;36(3-4):303–305. doi: 10.1042/bj0360303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. MAHLER H. R., ELOWE D. G. Studies on metalloflavoproteins. II. The rôle of iron in diphosphopyridine nucleotide cytochrome c reductase. J Biol Chem. 1954 Sep;210(1):165–179. [PubMed] [Google Scholar]
  11. PATWARDHAN M. V. Role of ferrous iron in enzymatic transamination. Nature. 1958 Jan 18;181(4603):187–187. doi: 10.1038/181187a0. [DOI] [PubMed] [Google Scholar]
  12. SALL T., RICHARDS H. K., HARRISON E., MYERSON R. M. A colorimetric procedure for the determination of serum glutamic oxalacetic transaminase. J Lab Clin Med. 1957 Aug;50(2):297–303. [PubMed] [Google Scholar]
  13. SRINIVASAN M. Effects of certain protein foods on blood-sugar levels and glucose tolerance. Lancet. 1957 Aug 17;273(6990):317–320. doi: 10.1016/s0140-6736(57)92209-2. [DOI] [PubMed] [Google Scholar]
  14. TONHAZY N. E., WHITE N. G., UMBREIT W. W. A rapid method for the estimation of the glutamic-aspartic transaminase in tissues and its application to radiation sickness. Arch Biochem. 1950 Aug;28(1):36–42. [PubMed] [Google Scholar]
  15. TULPULE P. G., PATWARDHAN V. N. Application of paper chromatography to the study of the transminase system. Nature. 1952 Apr 19;169(4303):671–671. doi: 10.1038/169671a0. [DOI] [PubMed] [Google Scholar]
  16. WOLFF J., WOLFF E. C. The effect of thyroxine on isolated dehydrogenases. Biochim Biophys Acta. 1957 Nov;26(2):387–396. doi: 10.1016/0006-3002(57)90021-5. [DOI] [PubMed] [Google Scholar]
  17. WOLFF J., WOLFF E. C. The effect of thyroxine on isolated dehydrogenases. Biochim Biophys Acta. 1957 Nov;26(2):387–396. doi: 10.1016/0006-3002(57)90021-5. [DOI] [PubMed] [Google Scholar]
  18. YANOFSKY C. D-Serine dehydrase of Neurospora. J Biol Chem. 1952 Sep;198(1):343–352. [PubMed] [Google Scholar]

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