Biophysical Characterization of Alanine Aminotransferase from Trypanosoma cruzi

Title:Biophysical Characterization of Alanine Aminotransferase from Trypanosoma cruzi

Volume: 23 Issue: 12

Author(s): Stephanie B. de Morais, Tatiana de Arruda Campos Brasil de Souza, Ana V.P. Weiler and Mario T. Murakami

Affiliation:

Keywords: Alanine aminotransferases, Trypanosoma cruzi, biophysical characterization, secondary structure, quaternary structure, enzyme.

Abstract: 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.

Cite this article as:

Morais B. de Stephanie, Arruda Campos Brasil de Souza de Tatiana, Weiler V.P. Ana and Murakami T. Mario, Biophysical Characterization of Alanine Aminotransferase from Trypanosoma cruzi, Protein & Peptide Letters 2016; 23 (12) . https://dx.doi.org/10.2174/0929866523666161025120511

DOI https://dx.doi.org/10.2174/0929866523666161025120511	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305