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