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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.
E F Skorkowski, and
K B Storey
January 1982,
Comparative biochemistry and physiology. B, Comparative biochemistry,
E F Skorkowski, and
K B Storey
October 1982,
Analytical biochemistry,
E F Skorkowski, and
K B Storey
September 1981,
Analytical biochemistry,
E F Skorkowski, and
K B Storey
October 1979,
Analytical biochemistry,
E F Skorkowski, and
K B Storey
July 1976,
FEBS letters,
E F Skorkowski, and
K B Storey
January 1979,
FEBS letters,
E F Skorkowski, and
K B Storey
August 1976,
Analytical biochemistry,
E F Skorkowski, and
K B Storey
December 1980,
Biochimica et biophysica acta,
E F Skorkowski, and
K B Storey
September 1982,
Analytical biochemistry,
E F Skorkowski, and
K B Storey
February 1981,
Carbohydrate research,
