The interaction of aliphatic and aromatic dicarboxylic acids with aspartate aminotransferase
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چکیده
منابع مشابه
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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1. The capacity ofvarious amino acids to convert the pyridoxal form ofaspartate aminotransferase into the pyridoxamine form has been investigated. 2. Glutamate has the highest converting capacity; aspartate, cx-aminopimelate, oc-aminoadipate and other amino acids follow. 3. The converting capacity of the various amino acids assayed is connected with their structural features. 4. A possible role...
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The binding of pyridoxamine 5-phosphate to the enzyme aspartate aminotransferase from pig heart was investigated by fluorescence spectroscopy. The substantial decrease in fluorescence intensity at 390 rnp that follows the interaction of pyridoxamine 5-phosphate with the apoenzyme was used to determine the alhnity constant. The effect of pH on the stability of the apoenzyme-pyridoxamine 5-phosph...
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Interaction of cytosolic apo-aspartate aminotransferase with AMP has been studied under equilibrium conditions; e.g., equilibrium dialysis and spectrophotometric titration. Results show that a 1:1 stoichiometric complex AMP-apo-aspartate aminotransferase monomer is formed. The calculated dissociation constants with the two different experimental techniques are 40.4 x 10(-6) M-1 and 31.4 x 10(-6...
متن کاملThe interaction between alpha-2-macroglobulin and cationic aspartate aminotransferase.
On starch-gel or polyacrylamide-gel electrophoresis of human serum, a supernumerary zone of aspartate aminotransferase activity may be demonstrated, migrating with the slow alpha(2) protein zone. This appearance is due only to cationic aspartate aminotransferase, bound by alpha(2)-macroglobulin. The binding is strongly potentiated by dilute borate buffers.
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1260020p