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Journal Abstract Search

149 related items for PubMed ID: 3162093

  • 1. [Study of the sorption immobilization of coenzyme-dependent oxidoreductases and their functions in electro-enzymatic processes and biological membranes].
    Shapovalov IuA, Gladyshev PP.
    Mol Biol (Mosk); 1985; 19(3):662-70. PubMed ID: 3162093
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  • 2. [Sorption immobilization of NAD-dependent enzyme systems. I. Influence of electrostatic interactions on the orientation of alcohol dehydrogenase on the sorbent surface].
    Gladyshev PP, Goriaev MI, Shpil'berg IG, Shapovalov IuA.
    Mol Biol (Mosk); 1982; 16(5):938-42. PubMed ID: 6755222
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  • 7. Binding of NADH to horse liver alcohol dehydrogenase: dependence on concentration of benzaldehyde and benzyl alcohol.
    Bignetti E.
    Physiol Chem Phys Med NMR; 1984; 16(1):21-7. PubMed ID: 6385034
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  • 8. Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase.
    Rubach JK, Plapp BV.
    Biochemistry; 2003 Mar 18; 42(10):2907-15. PubMed ID: 12627956
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  • 10. [A simple technic for immobilization of NAD+ preserving its coenzyme activity].
    Schöpp W, Lorenz R.
    Acta Biol Med Ger; 1980 Mar 18; 39(2-3):335-7. PubMed ID: 6999822
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  • 12. Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.
    Piersma SR, Visser AJ, de Vries S, Duine JA.
    Biochemistry; 1998 Mar 03; 37(9):3068-77. PubMed ID: 9485460
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  • 13. Electrochemistry of immobilized redox enzymes: kinetic characteristics of NADH oxidation catalysis at diaphorase monolayers affinity immobilized on electrodes.
    Limoges B, Marchal D, Mavré F, Savéant JM.
    J Am Chem Soc; 2006 Feb 15; 128(6):2084-92. PubMed ID: 16464111
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  • 20. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.
    Aufhammer SW, Warkentin E, Berk H, Shima S, Thauer RK, Ermler U.
    Structure; 2004 Mar 15; 12(3):361-70. PubMed ID: 15016352
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