Abstract
Methylene blue is converted to colourless leucomethylene blue in the presence of diaphorase and reduced nicotinamide adenine dinucleotide (NADH). Thus an enzyme reaction producing NADH can be monitored by visible semiconductor laser spectrometry of methylene blue, which has an absorption band in the red region at 670 nm. Lactate dehydrogenase (LDH) is determined by absorption spectrometry using a batch cell. A human serum sample containing 0.2 U ml −1 of LDH is easily detected in a reaction period of 5 min. A flow system is used to remove the effect of oxidation of leucomethylene blue by oxygen dissolved in the sample solution for quantitative analysis. Alcohol dehydrogenase is determined by fluorimetry down to 4 mU, the detection limit of ethanol being 10 nmol.
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