Purification, characterization and inhibition of d-3-aminoisobutyrate aminotransferase from the rat liver
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چکیده
منابع مشابه
Purification 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...
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We have purified CTP:phosphorylcholine cytidylyltransferase from rat liver cytosol 2180-fold to a specific activity of 12,250 nmol/min/mg of protein. The purified enzyme was stable at -70 degrees C in the presence of Triton X-100 and 0.2 M phosphate. The purified enzyme gave a single protein and activity band on nondenaturing polyacrylamide electrophoresis. Separation by sodium dodecyl sulfate-...
متن کاملPurification and characterization of a factor catalyzing the conversion of the multiple forms of tyrosine aminotransferase from rat liver.
Using glycerol as a stabilizing agent, a lysosomal factor (termed “convertase”) which converts the multiple forms of tyrosine aminotransferase has been purified about 16,000-fold with a 6% yield from rat liver. The purification method involves differential centrifugation, salt extraction of the mitochondrial-lysosomal fraction, acetone fractionation, acid precipitation, and chromatography on C...
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 کاملPurification and characterization of glycerophosphate acyltransferase from rat liver mitochondria.
Glycerophosphate acyltransferase (GAT) catalyzes the conversion of sn-glycerol 3-phosphate to lysophosphatidic acid (LPA), the first and committed step of triacylglycerol and phospholipid synthesis. In spite of the important regulatory roles GAT may play in this biosynthetic pathway, little information is available on the structure, biochemical properties, and regulation of GAT from eukaryotic ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1990
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1990.tb15457.x