RESUMO
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-ß 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.