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Influence of urea and organic solvents on the activity of immobilizedmyo-inositol-1-phosphate synthase containing active, self-regenerating coenzyme (NAD+) on the same matrix

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Abstract

myo-Inositol-1-phosphate synthase (EC 5.5.1.4.) from rat testes, an NAD+-containing enzyme that convertsd-glucose 6-phosphate to 1l-myo-inositol-1-phosphate was immobilized together with its cofactor and bovine serum albumin by crosslinking with glutaraldehyde at pH 4.5. The cofactor is reduced and reoxidized during the reaction cycle, thus forming a self-regenerating system with respect to the cofactor. The behavior of this immobilized enzyme/cofactor system in presence of organic solvents and urea and the activating effect of these compounds on the enzymatic activity were studied and discussed in the paper.

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Authors and Affiliations

  1. Institut für Allgemeine Biochemie der Universität Wien, Wien, Austria

    F. Pittner

  2. Ludwig-Boltzmann-Forschungsstelle für Biochemie, Wien, Austria

    F. Pittner

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  1. F. Pittner
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Pittner, F. Influence of urea and organic solvents on the activity of immobilizedmyo-inositol-1-phosphate synthase containing active, self-regenerating coenzyme (NAD+) on the same matrix. Appl Biochem Biotechnol 6, 153–166 (1981). https://doi.org/10.1007/BF02779247

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  • DOI: https://doi.org/10.1007/BF02779247

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