Aminotransferases are an important group of enzymes that catalyze the
transfer of an amino group of an amino acid into a keto acid. Alanine aminotransferase
from Trypanosoma cruzi (TcALAT) was cloned, overexpressed and purified.
Far-UV Circular Dichroism (CD), Dynamic Light Scattering (DLS), Analytical
Size Exclusion Chromatography (aSEC) and Small Angle X-ray Scattering
(SAXS) provide data concerning TcALAT biophysical behavior. CD analysis
displayed a typical spectrum of α-β proteins analogously as observed for other
alanine aminotransferases. The protein is stable until 40oC and above that temperature
starts to denatured. Its temperature of melting is equal to 50oC. DLS,
aSEC and SAXS data show that protein is monomeric in solution. All these gather
initial information on secondary and quaternary structures of TcALAT.
Keywords: Alanine aminotransferases, Trypanosoma cruzi, biophysical characterization, secondary structure, quaternary structure,
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