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Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase
Author(s) -
Kobayashi Tatsuhiko,
Nishii Masatoshi,
Takagi Yasuyuki,
Titani Koichi,
Matsuzawa Takeo
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81110-x
Subject(s) - ornithine aminotransferase , cloning (programming) , nucleic acid sequence , messenger rna , molecular cloning , ornithine , nucleotide , microbiology and biotechnology , chemistry , sequence analysis , biochemistry , sequence (biology) , biology , peptide sequence , gene , amino acid , arginine , computer science , programming language
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.