Molecular cloning of rat kynurenine aminotransferase: Identity with glutamine transaminase K
Autor: | Liviana Cozzi, Monica Mosca, Robert Schwarcz, Luca Benatti, Carmela Speciale, Etsuo Okuno, Jerome Breton |
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Rok vydání: | 1994 |
Předmět: |
DNA
Complementary Molecular Sequence Data Biophysics Lyases Biology Molecular cloning Kidney Biochemistry Cell Line chemistry.chemical_compound Kynurenic acid Structural Biology Complementary DNA Genetics Animals Coding region Amino Acid Sequence Cloning Molecular Molecular Biology Transaminases chemistry.chemical_classification Messenger RNA Kynurenine aminotransferase Base Sequence Excitatory amino acid Cell Biology Transfection Molecular biology Neuroprotection Rats Amino acid Enzyme chemistry Glutamine transaminase K Cysteine conjugate β-1yase |
Zdroj: | FEBS Letters. 353:21-24 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(94)01003-x |
Popis: | The enzyme kynurenine aminotransferase (KAT) catalyses the conversion of l-kynurenine to kynurenic acid. A combination of polymerase chain reaction techniques and hybridization screening was used to isolate a cDNA clone encompassing the entire coding region of KAT from rat kidney. Identification of the cDNA as coding for KAT was based both on the comparison of amino acid sequences obtained from purified rat KAT and on the expression of KAT activity in COS-1 cells transfected with the cDNA. RNA blot analysis indicated that KAT mRNA is widely expressed in rat tissues. Cultured cells transfected with the cDNA for KAT also showed glutamine transaminase K activity. Based mainly on sequence data, these results demonstrate that rat kidney KAT is identical with glutamine transaminase K. |
Databáze: | OpenAIRE |
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