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2. Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase

Author

Koichi Titani, Yasuyuki Takagi, Masatoshi Nishii, Tatsuhiko Kobayashi, and Takeo Matsuzawa

Subjects
Immunodiffusion, Pyridoxal phosphate binding site, animal structures, Sequence analysis, Ornithine aminotransferase, Molecular Sequence Data, Restriction Mapping, Biophysics, Molecular cloning, Biology, Kidney, (Human liver, Human kidney), Biochemistry, Isozyme, Structural Biology, Sequence Homology, Nucleic Acid, Complementary DNA, otorhinolaryngologic diseases, Genetics, medicine, Animals, Humans, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Molecular Biology, Transaminases, Base Sequence, Ornithine-Oxo-Acid Transaminase, cDNA library, fungi, Nucleic acid sequence, food and beverages, Cell Biology, Molecular biology, Rats, Isoenzymes, medicine.anatomical_structure, Genes, Liver, Pyridoxal Phosphate, cDNA, Nucleotide sequence
Abstract

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.

Published
1989
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