Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase
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چکیده
منابع مشابه
Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase.
Mitochondrial aspartate aminotransferase is inactivated irreversibly on heating. The inactivated protein aggregates, but aggregation is prevented by the presence of the chaperonin 60 from Escherichia coli (GroEL). The chaperonin increases the rate of thermal inactivation in the temperature range 55-65 degrees C but not at lower temperatures. It has previously been shown [Twomey and Doonan (1997...
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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...
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The kinetic behaviour of chicken liver and turkey liver aspartate aminotransferases (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) was studied. Steady-state data were obtained from a wide range of concentrations of substrates and product L-glutamate. The data were fitted by rational functions of degree 1:1, 1:2 and 2:2 with respect to substrates and 0:1, 1:1, 0:2 and 1:2 with regard ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1998
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3340219