Kobayashi T, Nishii M, Takagi Y, Titani K, Matsuzawa T
Department of Biochemistry, School of Medicine, Fujita-Gakuen Health University, Aichi, Japan.
FEBS Lett. 1989 Sep 25;255(2):300-4. doi: 10.1016/0014-5793(89)81110-x.
The cDNA encoding ornithine aminotransferase (EC 2.6.1.13; OAT) was isolated from a human kidney cDNA library. The isolated cDNA contained the entire protein coding region and partial 3'- and 5'-untranslated regions. The nucleotide sequences of human kidney OAT cDNA were absolutely homologous with those of human liver OAT cDNA, and human kidney and liver OAT fused completely against the antibody to human kidney OAT in an Ouchterlony double diffusion test. These findings settled the controversy as to which characteristics of liver and kidney OAT isozymes are different. An N-terminal sequence analysis of purified mature human kidney OAT clarified that the leader peptide was cleaved between Gln-35 and Gly-36.
从人肾cDNA文库中分离出编码鸟氨酸氨基转移酶(EC 2.6.1.13;OAT)的cDNA。分离出的cDNA包含完整的蛋白质编码区以及部分3'和5'非翻译区。人肾OAT cDNA的核苷酸序列与人肝OAT cDNA的序列完全同源,并且在免疫双扩散试验中,人肾和肝OAT与抗人肾OAT抗体完全融合。这些发现解决了关于肝和肾OAT同工酶哪些特征不同的争议。对纯化的成熟人肾OAT进行的N端序列分析表明,前导肽在Gln-35和Gly-36之间被切割。