Fukui K, Momoi K, Watanabe F, Miyake Y
Biochem Biophys Res Commun. 1986 Dec 30;141(3):1222-8. doi: 10.1016/s0006-291x(86)80175-9.
The biosynthesis of a porcine kidney peroxisomal enzyme, D-amino acid oxidase (EC 1.4.3.3., DAO), was investigated. Pig kidney mRNA as well as free and membrane-bound polysomes were used to investigate in vitro protein synthesis using a rabbit reticulocyte lysate. mRNA and free polysomes, but not membrane-bound polysomes, directed the synthesis of DAO. To examine the in vivo synthesis of the enzyme, a pig kidney cell line (LLC-PK1) was biosynthetically labelled. Both the in vitro and in vivo synthesized DAO had the same molecular weight, 38,000, as that of the purified enzyme. These results indicate strongly that DAO is synthesized on free ribosomes and transferred to the interior of peroxisomes without any proteolytic modification.
对猪肾过氧化物酶体酶D-氨基酸氧化酶（EC 1.4.3.3.，DAO）的生物合成进行了研究。使用猪肾mRNA以及游离和膜结合多核糖体，利用兔网织红细胞裂解物研究体外蛋白质合成。mRNA和游离多核糖体，而非膜结合多核糖体，指导了DAO的合成。为检测该酶的体内合成，对猪肾细胞系（LLC-PK1）进行生物合成标记。体外和体内合成的DAO分子量均与纯化酶相同，为38,000。这些结果有力地表明，DAO在游离核糖体上合成，并在没有任何蛋白水解修饰的情况下转移到过氧化物酶体内部。
