Resumen

CHANEZ-CARDENAS, María Elena  y  VAZQUEZ-CONTRERAS, Edgar. Two Notably Similar Proteins Follows Different Unfolding Pathways. Rev. Soc. Quím. Méx [online]. 2002, vol.46, n.3, pp.219-222. ISSN 0583-7693.

The amino acid sequences and the three dimensional structures of triosephosphate isomerase from the parasites Trypanosoma brucei and Trypanosoma cruzi, are markedly similar. In spite of these structural similarities, we found that the equilibrium unfolding pathway of both enzymes induced by guanidinium hydrochloride is different, as showed by alterations in intrinsic fluorescence of tryptophan residues. This behavior is possibly related with the different reactivity that these enzymes presents against derivatizing cysteine residues agents.

Palabras llave : Triosephosphate isomerase; three dimensional structures; proteines; unfolding pathway; fluorescence.

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