Abstract
The amount of soluble NADH-dependent malate dehydrogenase (MDH) activity extracted from maize was increased by increased nitrogen content of the growth medium. The effects of salts on MDH activity in vitro were investigated and shown to both stimulate (up to almost 4-fold) and inhibit total activity, depending on the salt concentration used. The changes in total activity were related to an alteration in the isoenzyme profiles eluted from Sephadex columns. This was due to an interconvertible variation in the molecular weight of the functional MDH molecule. The apparent K m of the predominant isoenzymes at given salt concentrations decreased as total MDH activity increased.
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