Abstract
We developed a continuous spectrofluorimetric assay of lysoplasmalogenase activity with the use of horse liver alcohol dehydrogenase as a coupling enzyme. In this method the disappearance of NADH is measured spectrofluorimetrically. The excitation and emission monochromators were set at 340 and 460 nm respectively. The assay is 10 times as sensitive as the previous u.v. spectrophotometric method. We could detect approx. 0.02 nmol of aldehyde produced/min per ml.
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