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Partial purification and characterization of a D-aminoacid oxidase from Octopus vulgaris hepatopancreas are described. An about 25-fold purification was achieved. The pH optimum was near to 9; molecular weight, determined by gel-filtration through G 200 Sephadex was approximately 55000; apparent Km was 10(-3)M. The enzyme showed great affinity for D-Ala and(More)
An enzymatic method for determination of Hg++ concentration is suggested. This method is based on the strong inhibitory effect of Hg++ on alcoholdehydrogenase (ADH). A correlation between per cent inhibition of ADH and [Hg++]/[ADH] was found. It was possible to determine [Hg++] in a range of values of [Hg++]/[ADH] from 1,58 to 72. A minimum Hg++(More)
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