Search Results - "Zeremski, J."

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  1. 1
    Bioorganic Mechanisms of the Formation of Free Radicals Catalyzed by Glucose Oxidase

    Bioorganic Mechanisms of the Formation of Free Radicals Catalyzed by Glucose Oxidase by Trivić, Svetlana, Leskovac, Vladimir, Zeremski, Jasmina, Vrvić, Miroslav, Winston, Gary W.

    Published in Bioorganic chemistry (01-04-2002)
    “…In this communication, we have described the activation of several xenobiotics by glucose oxidase from Aspergillus niger. The following compounds are readily…”
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  2. 2
    Novel substrates of yeast alcohol dehydrogenase ‐ 3. 4‐dimethylamino‐cinnamaldehyde and chloroacetaldehyde

    Novel substrates of yeast alcohol dehydrogenase ‐ 3. 4‐dimethylamino‐cinnamaldehyde and chloroacetaldehyde by Leskovac, V., Trivic, S., Zeremski, J., Stancic, B., Anderson, B. M.

    “…4‐Dimethylamino‐trans‐cinnamaldehyde and chloroacetaldehyde are novel substrates of yeast alcohol dehydrogenase (EC 1.1.1.1). In the present work, we have…”
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  3. 3
    chemical mechanism of action of glucose oxidase from Aspergillus niger

    chemical mechanism of action of glucose oxidase from Aspergillus niger by Wohlfahrt, G, Trivic, S, Zeremski, J, Pericin, D, Leskovac, V

    Published in Molecular and cellular biochemistry (01-05-2004)
    “…Glucose oxidase from Aspergillus niger (EC 1.1.3.4) is able to catalyze the oxidation of beta-D-glucose with p-benzoquinone, methyl-1,4-benzoquinone,…”
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  4. 4
    NAD super(+) binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentration

    NAD super(+) binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentration by Trivic, S, Zeremski, J, Leskovac, V

    Published in Biotechnology letters (01-08-1997)
    “…The pyrazole method of Theorell and Yonetani (Biochem. Z., 338: 573-553, 1963) has been adapted for the determination of the enzyme active site concentration…”
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  5. 5
    NAD+ binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentration

    NAD+ binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentration by Trivic, S, Zeremski, J, Leskovac, V

    Published in Biotechnology letters (1997)
    “…The pyrazole method of Theorell and Yonetani (Biochem. Z., 338: 537-553, 1963) has been adapted for the determination of the enzyme active site concentration…”
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  6. 6
    Influence of Tris(hydroxymethyl)aminomethane on kinetic mechanism of yeast alcohol dehydrogenase

    Influence of Tris(hydroxymethyl)aminomethane on kinetic mechanism of yeast alcohol dehydrogenase by Trivić, S, Leskovac, V, Zeremski, J, Stancić, B, Anderson, B M

    Published in Journal of enzyme inhibition (01-01-1998)
    “…Acetaldehyde, propionaldehyde, glyceraldehyde-3-P and 4-dimethylaminocinnamaldehyde form Schiff bases in Tris. HCl buffers; the rates of formation and…”
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