Abstract
On electrophoresis of whole cell extracts of Astasia longa we found two bands of NAD-dependent alcohol dehydrogenase activity (alcohol:NAD oxidoreductase EC 1.1.1.1) and one band of NADP-dependent alcohol dehydrogenase activity (alcohol:NADP oxidoreductase EC 1.1.1.2). These bands were termed alcohol dehydrogenase(NAD) I, alcohol dehydrogenase(NAD) II and alcohol dehydrogenase(NADP), respectively, in the order of their electrophoretic mobilities, alcohol dehydrogenase(NAD) I being the slowest moving component. Upon fractionation of the cells into a particulate and a cytosol fraction, we found that each fraction contained two bands corresponding to alcohol dehydrogenase(NAD) I and alcohol dehydrogenase(NAD) II when the gels were developed with ethanol and NAD as substrates. In the normal cells, alcohol dehydrogenase(NAD) II is predominant in the cytosol and very little alcohol dehydrogenase(NAD) I is seen. In the particulate fraction alcohol dehydrogenase(NAD) I is predominant. O 2 treatment and carbon deprivation increase the activity of alcohol dehydrogenase(NAD) I in the cytosol and this enzyme activity becomes the dominant activity in the cell. Some properties of these various alcohol dehydrogenase activities have been investigated.
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