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Journal Abstract Search

148 related items for PubMed ID: 1268221

  • 1.
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  • 2. The aromatic residue content of the enzyme rhodanese.
    Baillie RD, Horowitz PM.
    Biochim Biophys Acta; 1976 Apr 14; 427(2):594-9. PubMed ID: 1268220
    [Abstract] [Full Text] [Related]

  • 3. A physical characterization of sulfane sulfurtransferase.
    Aird BA, Horowitz PM.
    Biochim Biophys Acta; 1990 Mar 29; 1038(1):10-7. PubMed ID: 2317511
    [Abstract] [Full Text] [Related]

  • 4. Spectral differences between rhodanese catalytic intermediates unrelated to enzyme conformation.
    Chow SF, Horowitz PM.
    J Biol Chem; 1985 Aug 15; 260(17):9593-7. PubMed ID: 3860502
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  • 5. Contact versus energy transfer fluorescence quenching in the sulfur substituted form of the enzyme rhodanese: a study using cesium ion resolved emission spectra.
    Guido K, Horowitz PM.
    Biochem Biophys Res Commun; 1975 Nov 17; 67(2):670-6. PubMed ID: 1201046
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  • 6. Chemical modification of bovine liver rhodanese with tetrathionate: differential effects on the sulfur-free and sulfur-containing catalytic intermediates.
    Prasad AR, Horowitz PM.
    Biochim Biophys Acta; 1987 Jan 05; 911(1):102-8. PubMed ID: 3466649
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  • 9. A fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase.
    Wasylewski Z, Horowitz PM.
    Biochim Biophys Acta; 1982 Feb 04; 701(1):12-8. PubMed ID: 6948580
    [Abstract] [Full Text] [Related]

  • 10. Surface changes and role of buried water molecules during the sulfane sulfur transfer in rhodanese from Azotobacter vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study.
    Fasano M, Orsale M, Melino S, Nicolai E, Forlani F, Rosato N, Cicero D, Pagani S, Paci M.
    Biochemistry; 2003 Jul 22; 42(28):8550-7. PubMed ID: 12859202
    [Abstract] [Full Text] [Related]

  • 11. Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese.
    Horowitz P, Criscimagna NL.
    J Biol Chem; 1986 Nov 25; 261(33):15652-8. PubMed ID: 3465722
    [Abstract] [Full Text] [Related]

  • 12. Domain structural flexibility in rhodanese examined by quenching of a phosphorescent probe.
    Koloczek H, Vanderkooi JM.
    Biochim Biophys Acta; 1987 Nov 26; 916(2):236-44. PubMed ID: 2445385
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  • 14. Differential binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid to rhodanese catalytic intermediates.
    Horowitz PM, Criscimagna NL.
    Biochemistry; 1985 May 21; 24(11):2587-93. PubMed ID: 3861197
    [Abstract] [Full Text] [Related]

  • 15. Active site modifications quench intrinsic fluorescence of rhodanese by different mechanisms.
    Cannella C, Berni R, Rosato N, Finazzi-Agrò A.
    Biochemistry; 1986 Nov 18; 25(23):7319-23. PubMed ID: 3467793
    [Abstract] [Full Text] [Related]

  • 16. Selenium binding to beef-kidney rhodanese.
    Cannella C, Pecci L, Finazzi Agro A, Federici G, Pensa B, Cavallini D.
    Eur J Biochem; 1975 Jun 16; 55(1):285-9. PubMed ID: 1236798
    [Abstract] [Full Text] [Related]

  • 17. The structure of bovine liver rhodanese. II. The active site in the sulfur-substituted and the sulfur-free enzyme.
    Ploegman JH, Drent G, Kalk KH, Hol WG.
    J Mol Biol; 1979 Jan 15; 127(2):149-62. PubMed ID: 430559
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  • 20. The use of intrinsic protein fluorescence to quantitate enzyme-bound persulfide and to measure equilibria between intermediates in rhodanese catalysis.
    Horowitz P, Criscimagna NL.
    J Biol Chem; 1983 Jul 10; 258(13):7894-6. PubMed ID: 6575013
    [Abstract] [Full Text] [Related]

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