title: Purification and amino acid sequence of fructose-1,6-bisphosphate aldolase from the electric organ of Electrophorus electricus (L.).
abstract: 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.
authors.affiliation: Laboratório de Bioquímica de Proteínas e Peptídeos, Departamento de Bioquímica e Biologia Molecular, Instituto Oswaldo Cruz, FIOCRUZ, Av. Brasil 4365, 21045-900, Rio de Janeiro, RJ, Brasil. dsimone@ioc.fiocruz.br
authors.forename: Salvatore G
authors.initials: SG
authors.lastname: De-Simone
authors.forename: Christiane M Cardoso
authors.initials: CM
authors.lastname: de Salles
authors.forename: Celia M
authors.initials: CM
authors.lastname: Batista e Silva
authors.forename: Aida
authors.initials: A
authors.lastname: Hassón-Voloch
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D017124:Conserved Sequence; D004557:Electric Organ / Q000201:enzymology*; D004593:Electrophorus; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D005634:Fructose-Bisphosphate Aldolase