Aspartate aminotranferase from the thermophilic bacterium Thermus aquaticus has been purified to homogeneity. The enzyme is pyridoxal-5-phosphate dependent and is composed of two subunits having an Mr 44000 each. T. aquaticus AspAT shows a pI of 4.5 and is a thermophilic enzyme exhibiting its maximum activity at 80°C in the pH range 7-8. It is also resistant against denaturation to heat and several chemical agents.
Aspartate aminotranferase from the thermophilic bacterium Thermus aquaticus YT-1. Functional characterisation and stability
RAIMO, Gennaro;
1996-01-01
Abstract
Aspartate aminotranferase from the thermophilic bacterium Thermus aquaticus has been purified to homogeneity. The enzyme is pyridoxal-5-phosphate dependent and is composed of two subunits having an Mr 44000 each. T. aquaticus AspAT shows a pI of 4.5 and is a thermophilic enzyme exhibiting its maximum activity at 80°C in the pH range 7-8. It is also resistant against denaturation to heat and several chemical agents.File in questo prodotto:
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