Isolation and characterization of the rat tyrosine aminotransferase gene.
نویسندگان
چکیده
منابع مشابه
Isolation and characterization of the human tyrosine aminotransferase gene
Tyrosine aminotransferase (TAT; L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5) from rat liver is subject to glucocorticoid, cAMP, and developmental control. To study the underlying regulatory mechanisms, the TAT structural gene was isolated from a lambda bacteriophage rat DNA library. Heteroduplex analysis revealed that the 2.4-kilobase-long TAT mRNA is encoded by a gene that extends o...
متن کاملTyrosine Aminotransferase PURIFICATION AND CHARACTERIZATION
Tyrosine aminotransferase was highly purified from rat livers in which the enzyme had been induced by a glucocorticoid hormone. The preparation eluted from a DEAEcellulose column as a single peak gave a single precipitin line by the Ouchterlony double diffusion precipitin reaction and sedimented as a single boundary in the ultracentrifuge with an s20,W of 5.9. A molecular weight of 91,000 was d...
متن کاملParticipation of Ets transcription factors in the glucocorticoid response of the rat tyrosine aminotransferase gene.
We have previously shown that two remote glucocorticoid-responsive units (GRUs) of the rat tyrosine aminotransferase (TAT) gene contain multiple binding sites for several transcription factor families, including the glucocorticoid receptor (GR). We report here the identification of two novel binding sites for members of the Ets family of transcription factors in one of these GRUs. One of these ...
متن کاملPurification and properties of rat liver tyrosine aminotransferase.
Tyrosine aminotransferase (EC 2.6.1.5) of human liver was purified 2200-fold by successive chromatography on DEAE-cellulose DE-52, Ultrogel AcA-34, CM-Sephadex C-50 and hydroxyapatite to a specific activity of 64 units/mg of protein. The purified enzyme had a molecular mass of 95 500. The Km-values were 1.04 X 10(-3) mol/l, 0.17 X 10(-3) mol/l and 0.69 X 10(-6) mol/l for tyrosine, 2-oxoglutarat...
متن کاملTranscriptional activation of the rat liver tyrosine aminotransferase gene by cAMP.
The enzyme tyrosine aminotransferase (Tyr-ATase; L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5), which is synthesized in rat liver, is induced by glucocorticoids, insulin, and glucagon or its intracellular mediator cAMP. We have used cloned TyrATase genomic and cDNA sequences to study the mechanism of induction by cAMP. RNA blot analysis shows that cAMP causes a rapid 5-fold increase i...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1984
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.81.5.1346