Send to

Choose Destination

See 1 citation found using an alternative search:

J Chromatogr. 1987 Mar 13;389(2):427-32.

Affinity chromatography on 2',5'-ADP-Sepharose 4B for purification of malic enzyme from crustacean muscle.


Shrimp abdomenal muscle NADP-dependent malic enzyme (E.C. 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.

[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center