人肝脏中的酰基辅酶A合成酶与β-氧化的过氧化物酶体酶。其亚细胞定位的定量分析。
Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization.
作者信息
Bronfman M, Inestrosa N C, Nervi F O, Leighton F
出版信息
Biochem J. 1984 Dec 15;224(3):709-20. doi: 10.1042/bj2240709.
The presence of acyl-CoA synthetase (EC 6.2.1.3) in peroxisomes and the subcellular distribution of beta-oxidation enzymes in human liver were investigated by using a single-step fractionation method of whole liver homogenates in metrizamide continuous density gradients and a novel procedure of computer analysis of results. Peroxisomes were found to contain 16% of the liver palmitoyl-CoA synthetase activity, and 21% and 60% of the enzyme activity was localized in mitochondria and microsomal fractions respectively. Fatty acyl-CoA oxidase was localized exclusively in peroxisomes, confirming previous results. Human liver peroxisomes were found to contribute 13%, 17% and 11% of the liver activities of crotonase, beta-hydroxyacyl-CoA dehydrogenase and thiolase respectively. The absolute activities found in peroxisomes for the enzymes investigated suggest that in human liver fatty acyl-CoA oxidase is the rate-limiting enzyme of the peroxisomal beta-oxidation pathway, when palmitic acid is the substrate.
采用在甲泛葡胺连续密度梯度中对全肝匀浆进行单步分级分离的方法以及一种新的结果计算机分析程序，研究了过氧化物酶体中酰基辅酶A合成酶（EC 6.2.1.3）的存在情况以及人肝脏中β-氧化酶的亚细胞分布。发现过氧化物酶体含有肝脏棕榈酰辅酶A合成酶活性的16%，该酶活性的21%和60%分别定位于线粒体和微粒体部分。脂肪酰辅酶A氧化酶仅定位于过氧化物酶体，证实了先前的结果。发现人肝脏过氧化物酶体分别占肝脏巴豆酸酶、β-羟酰基辅酶A脱氢酶和硫解酶活性的13%、17%和11%。在所研究的酶中，过氧化物酶体中发现的绝对活性表明，当以棕榈酸为底物时，在人肝脏中脂肪酰辅酶A氧化酶是过氧化物酶体β-氧化途径的限速酶。
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