Abstract
In 1963 Mendicino and Vasarhely (1) first observed that fructose 1,6-diphosphatases from kidney and liver were specifically bound to cellulose phosphate and carboxymethylcellulose. These studies further clearly demonstrated that AMP and high concentrations of fructose 1,6-P2 inhibited the activity of the enzyme (1). Since this time a number of other workers have utilized the specific binding of this enzyme to anion exchange columns as the principal purification step in the isolation of the enzyme from a large number of different tissues (2,3,4,5).
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© 1974 Plenum Press, New York
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Mendicino, J., Abou-Issa, H. (1974). Cooperative Effects of AMP, ATP and Fructose 1,6-P2 on the Specific Elution of Fructose 1,6-Diphosphatase from Cellulose Phosphate. In: Dunlap, R.B. (eds) Immobilized Biochemicals and Affinity Chromatography. Advances in Experimental Medicine and Biology, vol 42. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6982-0_7
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DOI: https://doi.org/10.1007/978-1-4684-6982-0_7
Publisher Name: Springer, Boston, MA
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