过氧化物酶体参与豚鼠哈德氏腺脂质生物合成。
Participation of peroxisomes in lipid biosynthesis in the harderian gland of guinea pig.
作者信息
Horie S, Suga T
机构信息
Department of Clinical Biochemistry, Tokyo College of Pharmacy, Japan.
出版信息
Biochem J. 1989 Sep 1;262(2):677-80. doi: 10.1042/bj2620677.
Peroxisomal enzyme activities in the guinea-pig harderian gland, which has a unique lipid composition, were studied. Activities of catalase, acyl-CoA oxidase and the cyanide-insensitive acyl-CoA beta-oxidation system in this tissue were comparable with those in rat liver. The activities of dihydroxyacetone phosphate acyltransferase (DHAPAT, EC 2.3.1.42) and alkyl-DHAP synthase (EC 2.5.1.26) were appreciable, and the distributions of both activities were consistent with that of sedimentable catalase activity. Glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15), which is localized in both microsomes (microsomal fractions) and mitochondria in the rat liver, was a peroxisomal enzyme in the harderian gland, though the activity was only about one-tenth of the DHAPAT activity. These enzymes had different pH profiles and substrate specificity. The existence of high activities of enzymes of the acyl-DHAP pathway in peroxisomes suggests the physiological significance of peroxisomes in the biosynthesis of glycerol ether phospholipid and 1-alkyl-2,3-diacylglycerol in the guinea-pig harderian gland.
对具有独特脂质组成的豚鼠哈德氏腺中的过氧化物酶体酶活性进行了研究。该组织中过氧化氢酶、酰基辅酶A氧化酶和对氰化物不敏感的酰基辅酶Aβ-氧化系统的活性与大鼠肝脏中的相当。磷酸二羟丙酮酰基转移酶（DHAPAT，EC 2.3.1.42）和烷基-DHAP合酶（EC 2.5.1.26）的活性较高，且这两种活性的分布与可沉降的过氧化氢酶活性的分布一致。甘油-3-磷酸酰基转移酶（GPAT，EC 2.3.1.15）在大鼠肝脏中定位于微粒体（微粒体部分）和线粒体中，但在哈德氏腺中是一种过氧化物酶体酶，尽管其活性仅约为DHAPAT活性的十分之一。这些酶具有不同的pH谱和底物特异性。过氧化物酶体中酰基-DHAP途径的酶具有高活性，这表明过氧化物酶体在豚鼠哈德氏腺中甘油醚磷脂和1-烷基-2,3-二酰基甘油生物合成中的生理意义。
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