Title: Purification of Alcohol Dehydrogenase fromEntamoeba histolyticaandSaccharomyces cerevisiaeUsing Zinc-Affinity Chromatography
Abstract: We have developed a single-step method for the purification of NADP+-dependent alcohol dehydrogenase fromEntamoeba histolyticaand NAD+-dependent alcohol dehydrogenase fromSaccharomyces cerevisiae.It is based on the affinity for zinc of both enzymes. The amebic enzyme was purified almost 800 times with a recovery of 54% and the yeast enzyme was purified 30 times with a recovery of 100%. The kinetic constants of the purified enzymes were similar to those reported for other purification methods. With mammalian alcohol dehydrogenase, we obtained a 40-kDa band suggestive of purified alcohol dehydrogenase, but we failed to retain enzymatic activity in this preparation. Our results suggest that the described method is more applicable to the purification of tetrameric alcohol dehydrogenases.
Publication Year: 1997
Publication Date: 1997-08-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 6
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