The amino acid sequence of cytosolic aspartate aminotransferase from human liver
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Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
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The amino acid sequences of 39 tryptic peptides from carboxymethylated mitochondrial aspartate aminotransferase from pig heart muscle were analyzed. The peptides were purified by gel filtration, ion exchange column chromatography, paper chromatography, and high voltage paper electrophoresis, and their sequences were examined by manual Edman degradation, carboxypeptidase digestion, and fragmenta...
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The activity of aspartate aminotransferase (AST) in human serum has been widely determined as a diagnostic aid in liver disease. In this study, the effect of aluminium on AST isoenzymes in relation to aluminium intoxified patients has been investigated. Using gel filtration chromatography technique with Sephacryl S-300, mitochondrial aminotransferase (m-AST) and cytosolic aminotransferase (c-AS...
متن کاملchanges in the level of mitochondrial and cytosolic aspartate aminotransferase activities in aluminium intoxified rat
the activity of aspartate aminotransferase (ast) in human serum has been widely determined as a diagnostic aid in liver disease. in this study, the effect of aluminium on ast isoenzymes in relation to aluminium intoxified patients has been investigated. using gel filtration chromatography technique with sephacryl s-300, mitochondrial aminotransferase (m-ast) and cytosolic aminotransferase (c-as...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1990
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2700651