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  • Title: Affinity chromatography on 2',5'-ADP-Sepharose 4B for purification of malic enzyme from crustacean muscle.
    Author: Skorkowski EF, Storey KB.
    Journal: J Chromatogr; 1987 Mar 13; 389(2):427-32. PubMed ID: 3571365.
    Abstract:
    Shrimp abdomenal muscle NADP-dependent malic enzyme (E.C.1.1.1.40) was purified about 1500-fold to a specific activity of 48 units (mumol/min)/mg at 30 degrees C with good quantitative recovery in three chromatographic steps, including affinity chromatography on 2',5'-ADP-Sepharose 4B, a "substrate activation" method using malate substrate plus manganese chloride. In addition to the malate-manganese chloride substrate pair, succinate or glutamate plus manganese chloride or magnesium chloride could be used in this "substrate activation" method for crustacean NADP-malic enzyme purification on 2',5'-ADP-Sepharose 4B. Affinity chromatography alone purified malic enzyme almost 43 fold, and the overall method resulted in homogeneous enzyme since polyacrylamide gel electrophoresis of the native purified enzyme revealed only a single band staining for protein and enzyme activity.
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