Coupled optical rate determinations of amino acid oxidase activity

摘要: Abstract Methods are described in which liberation of ammonia from amino acid substrates by the d - and l -amino oxidases may be coupled with NADH-dependent reductive amination 2-oxoglutarate catalysed exogenous glutamate dehydrogenase ( -glutamate: NAD oxidoreductase (deaminating), EC 1.4.1.2). The inhibitin oxidase acid:O 2 1.4.3.3) ADP needed to activate stabilise was relieved FAD, substrate -alanine at approximately 6-fold K m concentration. Neither FAD or FMN were required 1.4.3.2) assay; this utilised -leucine as a concentration 7-fold value. methods reasonably sensitive precise, linear relationship between activity enzyme prevailed up an absorbance change 0.050 per min. They have advantage being amenable automation employment fluorescence techniques should greater sensitivity required.