Purification and amino acid sequence of fructose-1,6-bisphosphate aldolase from the electric organ of Electrophorus electricus (L.).
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.
De-Simone
Salvatore G
SG
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
de Salles
Christiane M Cardoso
CM
Batista e Silva
Celia M
CM
Hassón-Voloch
Aida
A
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
D005634:Fructose-Bisphosphate Aldolase