Department of Biochemistry, Weizmann Institute of Science, Rehovot, Israel.
Plant Physiol. 1977 Jan;59(1):15-7. doi: 10.1104/pp.59.1.15.
An enzyme catalyzing the phosphorylation of dihydroxyacetone has been identified in the halophilic alga, Dunaliella parva. Since glycerol and glyceraldehyde are not substrates, the enzyme is referred to as dihydroxyacetone kinase. Dihydroxyacetone kinase was purified 9-fold by ammonium sulfate fractionation followed by DEAE-cellulose chromatography.
已在嗜盐藻类小球藻中鉴定出一种催化二羟丙酮磷酸化的酶。由于甘油和甘油醛不是底物，因此该酶被称为二羟丙酮激酶。二羟丙酮激酶通过硫酸铵分级沉淀和 DEAE-纤维素层析进行 9 倍纯化。
