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PUBMED FOR HANDHELDS

Journal Abstract Search


135 related items for PubMed ID: 1092337

  • 1. 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
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  • 3. 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
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  • 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
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  • 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
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  • 6. The dissociated tryptophanase subunit is inactive.
    Raibaud O, Goldberg ME.
    J Biol Chem; 1976 May 10; 251(9):2820-4. PubMed ID: 770473
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  • 7. 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
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  • 8. Modification of tryptophanase with tetranitromethane.
    Nihira T, Toraya T, Fukui S.
    Eur J Biochem; 1981 Oct 10; 119(2):273-7. PubMed ID: 7030734
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  • 9. The folding characteristics of tryptophanase from Escherichia coli.
    Mizobata T, Kawata Y.
    J Biochem; 1995 Feb 10; 117(2):384-91. PubMed ID: 7608129
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  • 10. Catalytic function of a tyrosyl residue in tryptophanase.
    Kakizono T, Nihira T, Taguchi H.
    Biochem Biophys Res Commun; 1986 Jun 30; 137(3):964-9. PubMed ID: 3524569
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  • 11. Immobilization of pyridoxal 5'-phosphate and pyridoxal 5'-phosphate-dependent enzymes on Sepharose.
    Ikeda S, Fukui S.
    Methods Enzymol; 1979 Jun 30; 62():517-27. PubMed ID: 108513
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  • 18. 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
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  • 20. Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
    Ikushiro H, Hayashi H, Kawata Y, Kagamiyama H.
    Biochemistry; 1998 Mar 03; 37(9):3043-52. PubMed ID: 9485457
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