Purification and amino acid sequence of fructose-1,6-bisphosphate aldolase from the electric organ of Electrophorus electricus (L.).
نویسندگان
چکیده
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.
منابع مشابه
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ورودعنوان ژورنال:
- Zeitschrift fur Naturforschung. C, Journal of biosciences
دوره 61 11-12 شماره
صفحات -
تاریخ انتشار 2006