葡萄糖-6-磷酸脱氢酶和焦磷酸刺激的磷酸二羟丙酮酰基转移酶在小鼠肾脏中的过氧化物酶体定位。
Peroxisomal localization of glucose-6-phosphate dehydrogenase and pyrophosphate-stimulated dihydroxyacetone-phosphate acyltransferase in mouse kidney.
作者信息
Patel B N, Mackness M I, Connock M J
机构信息
Department of Biological Sciences, The Polytechnic, Wolverhampton, U.K.
出版信息
Biochem J. 1987 Jun 1;244(2):443-8. doi: 10.1042/bj2440443.
Abstract
- The subcellular localization of dihydroxyacetone-phosphate acyltransferase (DHAPAT) (assayed in the presence of pyrophosphate) and glucose-6-phosphate dehydrogenase (NADP+-dependent) activity in mouse kidney was investigated by density-gradient centrifugation. 2. DHAPAT has a predominantly peroxisomal distribution, and the activity in purified peroxisomes is stimulated by various organic and inorganic phosphate-containing compounds. The pH optimum is acid. 3. Approx. 10% of the cellular NADP+-dependent glucose-6-phosphate dehydrogenase activity is associated with peroxisomal fractions and may provide a source of NADPH for the peroxisomal reduction of acyl-dihydroxyacetone phosphate formed by DHAPAT activity.
摘要
- 通过密度梯度离心法研究了磷酸二羟丙酮酰基转移酶（DHAPAT）（在焦磷酸存在下测定）和葡萄糖-6-磷酸脱氢酶（依赖NADP⁺）在小鼠肾脏中的亚细胞定位。2. DHAPAT主要分布在过氧化物酶体中，纯化过氧化物酶体中的活性受到各种含有机和无机磷酸盐化合物的刺激。最适pH为酸性。3. 约10%的细胞依赖NADP⁺的葡萄糖-6-磷酸脱氢酶活性与过氧化物酶体组分相关，可能为DHAPAT活性形成的酰基二羟丙酮磷酸的过氧化物酶体还原提供NADPH来源。
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