Purification and amino acid sequence of fructose-1,6-bisphosphate aldolase from the electric organ of Electrophorus electricus (L.).
Z Naturforsch C J Biosci
; 61(11-12): 884-8, 2006.
Article
en En
| MEDLINE
| ID: mdl-17294701
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.
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Banco de datos:
MEDLINE
Asunto principal:
Órgano Eléctrico
/
Fructosa-Bifosfato Aldolasa
Límite:
Animals
Idioma:
En
Año:
2006
Tipo del documento:
Article