Purification and Amino Acid Sequence of Fructose-1,6-bisphosphate Aldolase from the Electric Organ of Electrophorus electricus (L.)

Salvatore G. De-Simone, Christiane M. Cardoso de Salles, Celia M. Batistae Silva, Aida Hassón-Voloch
2006 Zeitschrift für Naturforschung C - A Journal of Biosciences  
A soluble fructose-1,6-bisphosphate aldolase enzyme has been purified 50.2-fold (2.36%) at the homogeneity from the electric organ of Electrophorus electricus by one step of DEAE- 52 anion exchange chromatography followed by Superose-12 gel filtration-FPLC. Like other aldolase enzymes the E. electricus protein is a dimer with two identical subunits of 45 kDa. The N-terminal (20 residues) revealed a high homology with S. aurata (75%, goldfish), R. ratus and M. musculus (mouse, 80%) enzymes.
doi:10.1515/znc-2006-11-1217 fatcat:yghl6qam6fgorcboirgfnbwa2u