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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myo-Inositol-1-phosphate synthase (EC 18.104.22.168.) 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.
Index Entriesmyo-Inositol-1-phosphate NAD immobilized enzyme organic solvent, effect on immobilized enzyme activity urea, effect on immobilized enzyme activity coenzyme NAD+, self-regenerating regenerating, coenzyme NAD+ synthase,myo-inositol-1-phosphate
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