Abstract
Abstract It has been reported that treatment of amine-diamine oxidase mixtures with sodium borohydride resulted in the formation of a stable substrate-pyridoxal phosphate complex. When this procedure was applied to the bovine plasma amine oxidase in the presence of 14C-labeled substrate, the enzyme was inactivated and became radioactive. A pure radioactive product was isolated from acid hydrolyzates by ion exchange chromatography and preparative paper chromatography of the hydrolyzate. The compound was shown to be e-N-benzyllysine by mass spectrometry. This adduct was apparently a reduced intermediate in the catalytic pathway of substrate oxidation by the enzyme. Formation of a substrate-pyridoxal phosphate complex could not be confirmed.
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