Juan Luis Rendón Gómez, M.Sc.

Study of the glutathione reductase enzyme from Spirulina maxima

OBJECTIVES

• To characterize the kinetic and structural properties of glutathione reductase from Spirulina maxima.

SUMMARY

The project contemplates the study of the properties of glutathione reductase from the physico-chemical point of view. This enzyme plays an essential role in maintaining an adequate redox environment in the cell. The Spirulina enzyme is unusual with respect to the enzyme obtained from other sources in that it exhibits a tetrameric structure and is found in equilibrium with the dimeric species. The thermodynamics of this equilibrium and its dependence on pH have been characterized.

At present work is being done on the characterization of the denaturing behavior of the enzyme. The results obtained to date with guanidine hydrochloride and heat have revealed that the denaturing pattern followed by glutathione reductase is complex and the species obtained by thermal denaturation retains a significant level of structure.

PARTICIPANTS

• Dr.Guillermo Mendoza Hernández

BIBLIOGRAFIA

• 1. Rendón Juan L, Calcagno Mario, Mendoza-Hernández Guillermo and Ondarza Raúl N. (1986) Purification, Properties, and Oligomeric Structure of Glutathione Reductase from the Cyanobacterium Spirulina maxima. Archives of Biochemistry and Biophysics 248, (1) 215- 3.
• 2. Rendón Juan L and Mendoza-Hernández Guillermo. (1989) Dimer-Tetramer Equilibrium of Glutathione Reductase from the Cyanobacterium Spirulina maxima. Archives of Biochemistry and Biophysics 268 (1) 255-263.
• 3. Rendón Juan L and Mendoza-Hernández Guillermo. (1993) Effect of inorganic phosphate on the self-associating properties of glutathione reductase from Spirulina maxima. Biochemistry and Molecular Biology international 31 (4) 701-708.
• 4. Rendón Juan L, Pardo Juan P, Mendoza-Hernández Guillermo, Rojo-Domínguez Arturo and Hernández-Arana Andrés. (1995) Denaturing Behavior of Glutathione Reductase from Cyanobacterium Spirulina maxima in Guanidine Hydrochloride. Archives of Biochemistry and Biophysics 318 (2) 264-270.