Ghosh M K, Hajra A K
Arch Biochem Biophys. 1986 Mar;245(2):523-30. doi: 10.1016/0003-9861(86)90245-6.
On subcellular fractionation, the enzyme acyl/alkyl dihydroxyacetone phosphate (DHAP) reductase (EC 1.1.1.101) in guinea pig and rat liver was found to be present in both the light mitochondrial (L) and microsomal fractions. By using metrizamide density gradient centrifugation, it was shown that the alkyl DHAP reductase activity in the "L" fraction is localized mainly in peroxisomes. From the distribution of the marker enzymes it was calculated that about two-thirds of the liver reductase activity is in the peroxisomes and the rest in the microsomes. The properties of this enzyme in peroxisomes and microsomes are similar with respect to heat inactivation, pH optima, sensitivity to trypsin, and inhibition by NADP+ and acyl CoA. The enzyme activity in the peroxisomes and microsomes from mouse liver is increased to the same extent by chronically feeding the animals clofibrate, a hypolipidemic drug. The kinetic properties of this enzyme in these two different organelles are also similar. From these results it is concluded that the same enzyme is present in two different subcellular compartments of liver.
在亚细胞分级分离过程中,发现豚鼠和大鼠肝脏中的酰基/烷基二羟基丙酮磷酸(DHAP)还原酶(EC 1.1.1.101)存在于轻线粒体(L)和微粒体部分。通过使用甲泛葡胺密度梯度离心法,结果表明“L”部分中的烷基DHAP还原酶活性主要定位于过氧化物酶体。根据标记酶的分布计算得出,肝脏还原酶活性约三分之二存在于过氧化物酶体中,其余存在于微粒体中。该酶在过氧化物酶体和微粒体中的性质在热失活、最适pH、对胰蛋白酶的敏感性以及被NADP +和酰基辅酶A抑制方面相似。通过长期给动物喂食降血脂药物氯贝丁酯,小鼠肝脏过氧化物酶体和微粒体中的酶活性增加程度相同。该酶在这两种不同细胞器中的动力学性质也相似。从这些结果可以得出结论,肝脏的两个不同亚细胞区室中存在相同的酶。