Abstract
In order to inhibit the dimerization during the electrolytic reduction of nicotinamide adenine dinucleotide phosphate (NADP), NADP was covalently attached to a water-soluble polymer at proper intervals. Matrix-bound NADP was found to exhibit coenzymatic functions comparable to that of free NADP when it was coupled with glucose-6-phosphate dehydrogenase. According to the polarographic behaviors, matrix-bound NADP was electrolytically reduced at a controlled potential of -1.8 V vs. saturated calomel electrode (SCE). The electrolytically reduced product was identified as the enzymatically active NADPH by means of spectrophotometric and enzymatic assays. The dimerization of radical (NADP ) during the electrolytic reduction might be significantly retarded by immobilizing NADP to a water-soluble polymer matrix.
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Aizawa, M., Ikariyama, Y. & Suzuki, S. Nonenzymatic regeneration of NADPH from nadp in water-soluble polymer matrix-bound form. Journal of Solid-Phase Biochemistry 1, 249–259 (1976). https://doi.org/10.1007/BF02991024
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DOI: https://doi.org/10.1007/BF02991024