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unexpectedly low specific activity of a dehydrogenase

BabcockHall
in Biochemistry and Molecular Biology

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We are purifying a bacterial dehydrogenase from E. coli cells using a histidine tag. We purified the same dehydrogenase from different bacteria previously, and we have a few examples from the literature. The dehydrogenase from this organism is at least 100-fold lower in specific activity, perhaps more than that. We have a little experience with nickel columns, but not a great deal. Could a small amount of nickel ion be inhibiting our protein? We will try an experiment in which we incubate the enzyme with DTT shortly (there is an essential cysteine). What are other possible explanations?

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https://www.scienceforums.net/topic/140284-unexpectedly-low-specific-activity-of-a-dehydrogenase/
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