Abstract
Dihydroxyacetone kinase from Dunaliella salina is stabilized against inactivation by maintainance in the presence of 2 M glycerol. In the stabilized form a two-step purification procedure resulted in an enzyme preparation of about 440-fold purity which gave three bands (78 000–100 000 daltons) in the absence of denaturing agents on a polyacrylamide gel. The enzyme is specific for dihydroxyacetone and Mg 2+-ATP complex as its substrates. It has a sharp pH activity curve with a pH optimum around 7.5 and little activity below 6. It is suggested that dihydroxyacetone kinase plays a central role in the mechanism of osmoregulation via glycerol in Duneliella.
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