Article
Purification and Amino Acid Sequence of Fructose-1,6-bisphosphate Aldolase from the Electric Organ of Electrophorus electricus (L.)
Registro en:
DE SIMONE, Salvatore G. et al. Purification and Amino Acid Sequence of Fructose-1,6-bisphosphate Aldolase from the Electric Organ of Electrophorus electricus (L.). Z. Naturforsch C J Biosci, v. 61, n. 11-12, p. 884-888, Nov./Dec. 2006.
0939-5075
10.1515/znc-2006-11-1217
Autor
De Simone, Salvatore G.
Salles, Christiane M. Cardoso de
Silva, Celia M. Batista e
Hassón-Voloch, Aida
Resumen
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. 2022-01-01