Thermal-unfolding reaction of triosephosphate isomerase from Trypanosoma cruzi.
Thermal denaturation of triosephosphate isomerase from Trypanosoma cruzi was studied by circular dicrhoism and fluorescence spectroscopies. The unfolding transition was found to be highly irreversible even at the very early stages of the reaction. Kinetic studies, allowed us to identify consecutive reactions. Firstly, only the tryptophan environment is altered. Next, changes on the secondary structure and hydrophobic surface exposure measured by 1-anilino-8-naphthalenesulfonate (ANS) binding were observed. Further conformational changes imply additional modifications on the secondary and tertiary structures and release of the hydrophobic dye leading to the formation of the unfolded state that is prone to aggregate.
Mixcoha-Hernández
Edgar
E
Laboratorio de Investigación Bioquímica, Programa Institucional en Biomedicina Molecular ENMyH-IPN, Guillermo Massieu Helguera No. 239, La Escalera Ticoman, 07320, D.F, Mexico.
Moreno-Vargas
Liliana M
LM
Rojo-Domínguez
Arturo
A
Benítez-Cardoza
Claudia G
CG
D000817:Anilino Naphthalenesulfonates / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D007700:Kinetics; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014305:Triose-Phosphate Isomerase / Q000737:chemistry*; D014349:Trypanosoma cruzi / Q000201:enzymology*
D000817:Anilino Naphthalenesulfonates; C027132:1-anilino-8-naphthalenesulfonate; D014305:Triose-Phosphate Isomerase