Purification and Amino Acid Sequence of Fructose-1,6-bisphosphate Aldolase from the Electric Organ of Electrophorus electricus (L.)

dc.creatorDe Simone, Salvatore G.
dc.creatorSalles, Christiane M. Cardoso de
dc.creatorSilva, Celia M. Batista e
dc.creatorHassón-Voloch, Aida
dc.date2020-01-16T12:48:06Z
dc.date2020-01-16T12:48:06Z
dc.date2006
dc.date.accessioned2023-09-26T22:14:30Z
dc.date.available2023-09-26T22:14:30Z
dc.identifierDE 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.
dc.identifier0939-5075
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/39252
dc.identifier10.1515/znc-2006-11-1217
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8876710
dc.descriptionA 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.
dc.description2022-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherVerlag
dc.rightsrestricted access
dc.subjectFrutose-1,6-bifosfato Aldolase
dc.subjectPurificação e sequência de aminoácidos
dc.subjectElectrophorus electricus
dc.subjectFructose-1,6-bisphosphate Aldolase
dc.subjectElectrophorus electricus (L.)
dc.subjectPurification
dc.titlePurification and Amino Acid Sequence of Fructose-1,6-bisphosphate Aldolase from the Electric Organ of Electrophorus electricus (L.)
dc.typeArticle


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