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Journal Abstract Search

93 related items for PubMed ID: 321224

  • 1. The reactivity of one essential cysteine as a conformational probe in Escherichia coli tryptophanase. Application to the study of the structural influence of subunit interactions.
    Raibaud O, Goldberg ME.
    Eur J Biochem; 1977 Mar 01; 73(2):591-9. PubMed ID: 321224
    [Abstract] [Full Text] [Related]

  • 2. Effects of temperature and monovalent cations on activity and quaternary structure of tryptophanase.
    Honda T, Tokushige M.
    J Biochem; 1986 Sep 01; 100(3):679-85. PubMed ID: 3536895
    [Abstract] [Full Text] [Related]

  • 3. The dissociated tryptophanase subunit is inactive.
    Raibaud O, Goldberg ME.
    J Biol Chem; 1976 May 10; 251(9):2820-4. PubMed ID: 770473
    [Abstract] [Full Text] [Related]

  • 4. Essential arginine residues in tryptophanase from Escherichia coli.
    Kazarinoff MN, Snell EE.
    J Biol Chem; 1977 Nov 10; 252(21):7598-602. PubMed ID: 334762
    [Abstract] [Full Text] [Related]

  • 5. Kinetic and equilibrium studies on the activation of Escherichia coli K12 tryptophanase by pyridoxal 5'-phosphate and monovalent cations.
    Högberg-Raibaud A, Raibaud O, Goldberg ME.
    J Biol Chem; 1975 May 10; 250(9):3352-8. PubMed ID: 1091651
    [Abstract] [Full Text] [Related]

  • 6. Cleavage of Escherichia coli tryptophan indole-lyase by trypsin at Lys406 affects the transmission of conformational changes associated with monovalent cation activation.
    Phillips RS, Doshi KJ.
    Eur J Biochem; 1998 Jul 15; 255(2):508-15. PubMed ID: 9716394
    [Abstract] [Full Text] [Related]

  • 7. Functional role of cysteinyl residues in tryptophanase.
    Nihira T, Yasuda T, Kakizono T, Taguchi H, Ichikawa M, Toraya T, Fukui S.
    Eur J Biochem; 1985 May 15; 149(1):129-33. PubMed ID: 3888623
    [Abstract] [Full Text] [Related]

  • 8. Role of cysteine residues in tryptophanase for monovalent cation-induced activation.
    Tokushige M, Tsujimoto N, Oda T, Honda T, Yumoto N, Ito S, Yamamoto M, Kim EH, Hiragi Y.
    Biochimie; 1989 Jun 15; 71(6):711-20. PubMed ID: 2502187
    [Abstract] [Full Text] [Related]

  • 9. Kinetic studies on coenzyme binding and coenzyme dissociation in tryptophanase immobilized on sepharose.
    Ikeda S, Sumi Y, Fukui S.
    Biochemistry; 1975 Apr 08; 14(7):1464-70. PubMed ID: 1092337
    [Abstract] [Full Text] [Related]

  • 10. Modification of tryptophanase with tetranitromethane.
    Nihira T, Toraya T, Fukui S.
    Eur J Biochem; 1981 Oct 08; 119(2):273-7. PubMed ID: 7030734
    [Abstract] [Full Text] [Related]

  • 11. Comparative studies on the properties of tryptophanase and tyrosine phenol-lyase immobilized directly on Sepharose or by use of Sepharose-bound pyridoxal 5'-phosphate.
    Fukui S, Ikeda S, Fujimura M, Yamada H, Kumagai H.
    Eur J Biochem; 1975 Feb 03; 51(1):155-64. PubMed ID: 1091485
    [Abstract] [Full Text] [Related]

  • 12. Temperature-dependent structural rearrangement of apotryptophanase in potassium phosphate.
    Lachmann G, Schnackerz KD.
    Biochim Biophys Acta; 1985 Oct 18; 831(3):275-80. PubMed ID: 3902088
    [Abstract] [Full Text] [Related]

  • 13. Pyridoxal 5'-phosphate and analogs as probes of coenzyme-protein interaction in Baccillus alvei tryptophanase.
    Isom HC, DeMoss RD.
    Biochemistry; 1975 Sep 23; 14(19):4291-7. PubMed ID: 241380
    [Abstract] [Full Text] [Related]

  • 14. Monovalent cation activation of tryptophanase.
    Suelter CH, Snell EE.
    J Biol Chem; 1977 Mar 25; 252(6):1852-7. PubMed ID: 321445
    [Abstract] [Full Text] [Related]

  • 15. Structural and functional interdependence of the protomers of Escherichia coli K 12 tryptophanase during binding of pyridoxal 5'-phosphate.
    Raibaud O, Goldberg ME.
    J Biol Chem; 1976 May 10; 251(9):2814-9. PubMed ID: 770472
    [Abstract] [Full Text] [Related]

  • 16. Evidence that cysteine 298 is in the active site of tryptophan indole-lyase.
    Phillips RS, Gollnick PD.
    J Biol Chem; 1989 Jun 25; 264(18):10627-32. PubMed ID: 2659590
    [Abstract] [Full Text] [Related]

  • 17. Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: unraveling the cold inactivation.
    Erez T, Phillips RS, Parola AH.
    FEBS Lett; 1998 Aug 21; 433(3):279-82. PubMed ID: 9744811
    [Abstract] [Full Text] [Related]

  • 18. The tryptophanase from Escherichia coli K12. 3. Further characterization of hybrids between the apo- and holoenzyme.
    Skrzynia C, London J, Goldberg ME.
    J Biol Chem; 1974 Apr 10; 249(7):2325-6. PubMed ID: 4594500
    [No Abstract] [Full Text] [Related]

  • 19. Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.
    Erez T, Gdalevsky GYa, Torchinsky YM, Phillips RS, Parola AH.
    Biochim Biophys Acta; 1998 May 19; 1384(2):365-72. PubMed ID: 9659398
    [Abstract] [Full Text] [Related]

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