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. electri...

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Published inZeitschrift für Naturforschung C. A journal of biosciences Vol. 61; no. 11; pp. 884 - 888
Main Authors De-Simone, Salvatore G., Salles, Christiane M. Cardoso de, Silva, Celia M. Batistae, Hassón-Voloch, Aida
Format Journal Article
LanguageEnglish
Published Germany Verlag der Zeitschrift für Naturforschung 01.11.2006
Subjects
Amino Acid Sequence
Animals
Chromatography, Ion Exchange
Conserved Sequence
Electric Organ - enzymology
Electrophorus
Electrophorus electricus (L.)
Fructose-1,6-bisphosphate Aldolase
Fructose-Bisphosphate Aldolase - chemistry
Fructose-Bisphosphate Aldolase - genetics
Fructose-Bisphosphate Aldolase - isolation & purification
Molecular Sequence Data
Purification
Sequence Alignment
Sequence Homology, Amino Acid
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0939-5075
1865-7125
DOI:10.1515/znc-2006-11-1217